K. C. Neuman, A. Nagy, A. A. Deniz, S. Mukhopadhyay, and E. A. Lemke, Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy Single-molecule biophysics: at the interface of biology, physics and chemistry, Bibliography Nat. Methods J. R. Soc. Interface Phys. Rev. Lett, vol.5, issue.56, pp.491-505, 1986.

A. Ashkin, J. M. Dziedzic, J. E. Bjorkholm, S. Chu, F. Pillet et al., Observation of a single-beam gradient force optical trap for dielectric particles Atomic Force Microscopy and pharmacology: From microbiology to cancerology Nanoscale analysis of the effects of antibiotics and CX1 on a Pseudomonas aeruginosa multidrug-resistant strain, Nanoscale Adhesion Forces of Pseudomonas aeruginosa Type IV Pili, pp.1028-1050, 1986.

L. I. Abu-lail, Y. Liu, A. Atabek, and T. A. Camesano, and Natural Organic Matter, Environmental Science & Technology, vol.41, issue.23, pp.8031-8037, 2007.
DOI : 10.1021/es071047o

I. E. Ivanov, E. N. Kintz, L. A. Porter, J. B. Goldberg, N. A. Burnham et al., Relating the Physical Properties of Pseudomonas aeruginosa Lipopolysaccharides to Virulence by Atomic Force Microscopy, Journal of Bacteriology, vol.193, issue.5, pp.1259-1266, 2011.
DOI : 10.1128/JB.01308-10

A. Touhami, M. H. Jericho, J. M. Boyd, and T. J. Beveridge, Nanoscale Characterization and Determination of Adhesion Forces of Pseudomonas aeruginosa Pili by Using Atomic Force Microscopy, Journal of Bacteriology, vol.188, issue.2, pp.370-377, 2006.
DOI : 10.1128/JB.188.2.370-377.2006

P. Tripathi, A. Beaussart, D. Alsteens, V. Dupres, I. Claes et al., Adhesion and Nanomechanics of Pili from the Probiotic Lactobacillus rhamnosus GG, ACS Nano, vol.7, issue.4, pp.3685-97, 2013.
DOI : 10.1021/nn400705u

T. Bjarnsholt, P. Ø. Jensen, T. H. Jakobsen, R. Phipps, A. K. Nielsen et al., Quorum Sensing and Virulence of Pseudomonas aeruginosa during Lung Infection of Cystic Fibrosis Patients, PLoS ONE, vol.5, issue.4, pp.1-10, 2010.
DOI : 10.1371/journal.pone.0010115.t001

M. Hentzer and M. Givskov, Pharmacological inhibition of quorum sensing for the treatment of chronic bacterial infections, Journal of Clinical Investigation, vol.112, issue.9, pp.1300-1307, 2003.
DOI : 10.1172/JCI20074

S. P. Diggle, R. E. Stacey, C. Dodd, M. Cámara, P. Williams et al., The galactophilic lectin, LecA, contributes to biofilm development in Pseudomonas aeruginosa, Environmental Microbiology, vol.336, issue.6, pp.1095-1104, 2006.
DOI : 10.1126/science.1112422

A. Imberty, M. Wimmerová, E. P. Mitchell, and N. Gilboa-garber, Structures of the lectins from Pseudomonas aeruginosa: insights into the molecular basis for host glycan recognition, Microbes and Infection, vol.6, issue.2, pp.221-228, 2004.
DOI : 10.1016/j.micinf.2003.10.016
URL : https://hal.archives-ouvertes.fr/hal-00306814

C. Chemani, A. Imberty, S. De-bentzmann, M. Pierre, M. Wimmerová et al., Role of LecA and LecB Lectins in Pseudomonas aeruginosa-Induced Lung Injury and Effect of Carbohydrate Ligands, Infection and Immunity, vol.77, issue.5, pp.2065-2075, 2009.
DOI : 10.1128/IAI.01204-08
URL : https://hal.archives-ouvertes.fr/hal-00396635

B. Blanchard, A. Nurisso, E. Hollville, C. Tétaud, J. Wiels et al., Structural Basis of the Preferential Binding for Globo-Series Glycosphingolipids Displayed by Pseudomonas aeruginosa Lectin I, Journal of Molecular Biology, vol.383, issue.4, pp.837-853, 2008.
DOI : 10.1016/j.jmb.2008.08.028
URL : https://hal.archives-ouvertes.fr/hal-00352496

A. Imberty, Y. M. Chabre, and R. Roy, Glycomimetics and Glycodendrimers as High Affinity Microbial Anti-adhesins, Chemistry - A European Journal, vol.580, issue.25, pp.7490-7499, 2008.
DOI : 10.4052/tigg.16.243

S. Cecioni, A. Imberty, and S. Vidal, Glycomimetics versus Multivalent Glycoconjugates for the Design of High Affinity Lectin Ligands, Chemical Reviews, vol.115, issue.1, pp.525-561, 2015.
DOI : 10.1021/cr500303t
URL : https://hal.archives-ouvertes.fr/hal-01146938

J. J. Lundquist and E. J. Toone, The Cluster Glycoside Effect, Chemical Reviews, vol.102, issue.2, pp.555-578, 2002.
DOI : 10.1021/cr000418f

F. Pertici and R. J. Pieters, Potent divalent inhibitors with rigid glucose click spacers for Pseudomonas aeruginosa lectin LecA, Chemical Communications, vol.17, issue.33, pp.4008-4010, 2012.
DOI : 10.1002/chem.201003402

F. Casoni, L. Dupin, G. Vergoten, A. Meyer, C. Ligeour et al., The influence of the aromatic aglycon of galactoclusters on the binding of LecA: a case study with O-phenyl, S-phenyl, O-benzyl, S-benzyl, O-biphenyl and O-naphthyl aglycons, Org. Biomol. Chem., vol.108, issue.45, pp.9166-9179, 2014.
DOI : 10.1021/jp031178l
URL : https://hal.archives-ouvertes.fr/hal-01084164

B. Gerland, A. Goudot, C. Ligeour, G. Pourceau, A. Meyer et al., Structure Binding Relationship of Galactosylated Glycoclusters toward Pseudomonas aeruginosa Lectin LecA Using a DNA-Based Carbohydrate Microarray, Bioconjugate Chemistry, vol.25, issue.2, pp.379-392, 2014.
DOI : 10.1021/bc4005365
URL : https://hal.archives-ouvertes.fr/hal-00952679

M. A. Boukareb, Lung Infection, Journal of Medicinal Chemistry, vol.57, issue.24, pp.10275-10289, 2014.
DOI : 10.1021/jm500038p

L. Dupin, Validation et criblage de nouvelles molécules anti-infectieuses sur microarray : applications à Pseudomonas aeruginosa, 2016.

B. Stuart, J. H. Lin, and P. J. Jr, Early Eradication of Pseudomonas aeruginosa in Patients with Cystic Fibrosis, Paediatric Respiratory Reviews, vol.11, issue.3, pp.177-184, 2010.
DOI : 10.1016/j.prrv.2010.05.003

S. Moreau-marquis, B. A. Stanton, and G. A. O-'toole, Pseudomonas aeruginosa biofilm formation in the cystic fibrosis airway, Pulmonary Pharmacology & Therapeutics, vol.21, issue.4, pp.595-599, 2008.
DOI : 10.1016/j.pupt.2007.12.001

O. Sullivan, B. P. Freedman, and S. D. Cystic-fibrosis, Cystic fibrosis, The Lancet, vol.373, issue.9678, pp.1891-1904, 2009.
DOI : 10.1016/S0140-6736(09)60327-5

R. L. Gibson, J. L. Burns, and B. W. Ramsey, Pathophysiology and Management of Pulmonary Infections in Cystic Fibrosis, American Journal of Respiratory and Critical Care Medicine, vol.168, issue.8, pp.918-951, 2003.
DOI : 10.1080/21548331.1997.11443512

K. N. Cowles, T. S. Moser, A. Siryaporn, N. Nyakudarika, W. Dixon et al., polar motility mechanisms, Molecular Microbiology, vol.184, issue.5, pp.923-938, 2013.
DOI : 10.1111/j.1574-6968.2000.tb09002.x
URL : http://onlinelibrary.wiley.com/doi/10.1111/mmi.12403/pdf

J. W. Costerton, P. S. Stewart, and E. P. Greenberg, Bacterial Biofilms: A Common Cause of Persistent Infections, Science, vol.284, issue.5418, pp.1318-1322, 1999.
DOI : 10.1126/science.284.5418.1318

N. Hoiby, T. Bjarnsholt, M. Givskov, S. Molin, and O. Ciofu, Antibiotic resistance of bacterial biofilms, International Journal of Antimicrobial Agents, vol.35, issue.4, pp.322-332, 2010.
DOI : 10.1016/j.ijantimicag.2009.12.011
URL : https://hal.archives-ouvertes.fr/hal-00567285

M. Feldman, R. Bryan, S. Rajan, L. Scheffler, S. Brunnert et al., Role of Flagella in Pathogenesis of Pseudomonas aeruginosa Pulmonary Infection Role of Flagella in Pathogenesis of Pseudomonas aeruginosa Pulmonary Infection, pp.43-51, 1998.

N. Mcnamara, M. Gallup, A. Sucher, I. Maltseva, D. Mckemy et al., AsialoGM1 and TLR5 Cooperate in Flagellin-Induced Nucleotide Signaling to Activate Erk1/2, American Journal of Respiratory Cell and Molecular Biology, vol.34, issue.6, pp.653-660, 2006.
DOI : 10.1074/jbc.M411875200

A. Scharfman, S. K. Arora, P. Delmotte, E. Van-brussel, J. Mazurier et al., Recognition of Lewis x Derivatives Present on Mucins by Flagellar Components of Pseudomonas aeruginosa, Infection and Immunity, vol.69, issue.9, pp.5243-5248, 2001.
DOI : 10.1128/IAI.69.9.5243-5248.2001
URL : https://hal.archives-ouvertes.fr/hal-00149469

E. Mahenthiralingam, M. E. Campbell, and D. P. Speert, Nonmotility and phagocytic resistance of Pseudomonas aeruginosa isolates from chronically colonized patients with cystic Nonmotility and Phagocytic Resistance of Pseudomonas aeruginosa Isolates from Chronically Colonized Patients with Cystic Fibrosis, pp.596-605, 1994.

D. E. Bradley, PAO polar pili: twitching motility, Canadian Journal of Microbiology, vol.26, issue.2, pp.146-154, 1980.
DOI : 10.1139/m80-022

J. M. Skerker and H. C. Berg, Direct observation of extension and retraction of type IV pili, Proceedings of the National Academy of Sciences, vol.19, issue.13, pp.6901-6905, 2001.
DOI : 10.1093/emboj/19.13.3223

J. Kocourek and V. Horejsí, Defining a lectin, Nature, vol.290, issue.5803, 1981.
DOI : 10.1038/290188a0

J. Glick and N. Garber, The Intracellular Localization of Pseudomonas aeruginosa Lectins, Microbiology, vol.129, issue.10, pp.3085-3090, 1983.
DOI : 10.1099/00221287-129-10-3085

N. Gilboa-garber, Multiple aspects of Pseudomonas aeruginosa lectins, Acta Leopoldina NF, vol.75, pp.153-177, 1997.

S. Kirkeby, A. K. Hansen, A. D-'apice, and D. Moe, The galactophilic lectin (PA-IL, gene LecA) from Pseudomonas aeruginosa. Its binding requirements and the localization of lectin receptors in various mouse tissues, Microbial Pathogenesis, vol.40, issue.5, pp.191-197, 2006.
DOI : 10.1016/j.micpath.2006.01.006

R. Loris, D. Tielker, K. E. Jaeger, and L. Wyns, Structural Basis of Carbohydrate Recognition by the Lectin LecB from Pseudomonas aeruginosa, Journal of Molecular Biology, vol.331, issue.4, pp.861-870, 2003.
DOI : 10.1016/S0022-2836(03)00754-X

O. Bajolet-laudinat, S. Girod-de-bentzmann, J. M. Tournier, C. Madoulet, M. Plotkowski et al., Cytotoxicity of Pseudomonas aeruginosa Internal Lectin PA-I to Respiratory Epithelial Cells in Primary Culture, Infect. Immun, vol.62, pp.4481-4487, 1994.

T. Eierhoff, B. Bastian, R. Thuenauer, J. Madl, A. Audfray et al., A lipid zipper triggers bacterial invasion, Proceedings of the National Academy of Sciences, vol.70, issue.3, pp.6-11, 2014.
DOI : 10.1016/S0006-3495(96)79693-5
URL : https://hal.archives-ouvertes.fr/hal-01066717

R. S. Laughlin, M. W. Musch, C. J. Hollbrook, F. M. Rocha, E. B. Chang et al., The Key Role of Pseudomonas aeruginosa PA-I Lectin on Experimental Gut-Derived Sepsis, Annals of Surgery, vol.232, issue.1
DOI : 10.1097/00000658-200007000-00019

A. Bernardi, Multivalent glycoconjugates as anti-pathogenic agents, Chem. Soc. Rev., vol.4, issue.11, pp.4709-4736, 2013.
DOI : 10.1002/cmdc.200800380
URL : https://hal.archives-ouvertes.fr/hal-01326075

C. Ryder, M. Byrd, and D. J. Wozniak, Role of polysaccharides in Pseudomonas aeruginosa biofilm development, Current Opinion in Microbiology, vol.10, issue.6, pp.644-648, 2007.
DOI : 10.1016/j.mib.2007.09.010

B. Haj-khalifa, A. Moissenet, D. Vu-thien, H. Khedher, and M. , Virulence factors in Pseudomonas aeruginosa: mechanisms and modes of regulation, Ann. Biol. Clin, vol.69, pp.393-403, 2011.

B. Pritt, L. O-'brien, and W. Winn, in Cystic Fibrosis, American Journal of Clinical Pathology, vol.128, issue.1, pp.32-34, 2007.
DOI : 10.1309/KJRPC7DD5TR9NTDM

I. W. Sutherland, Biofilm exopolysaccharides: a strong and sticky framework, Microbiology, vol.147, issue.1, pp.3-9, 2001.
DOI : 10.1099/00221287-147-1-3

M. Lahmann, Architectures of Multivalent Glycomimetics for Probing Carbohydrate???Lectin Interactions, Top Curr Chem, vol.288, pp.17-65, 2009.
DOI : 10.1007/128_2008_30

Y. M. Chabre and R. Roy, Multivalent glycoconjugate syntheses and applications using aromatic scaffolds, Chemical Society Reviews, vol.12, issue.11, pp.4657-708, 2013.
DOI : 10.1002/chem.200500901

M. Reynolds and S. Pérez, Thermodynamics and chemical characterization of protein???carbohydrate interactions: The multivalency issue, Comptes Rendus Chimie, vol.14, issue.1, pp.74-95, 2011.
DOI : 10.1016/j.crci.2010.05.020
URL : https://hal.archives-ouvertes.fr/hal-00577113

K. D. Zinger-yosovich and N. Gilboa-garber, Lectins by Plant and Microbial Branched Polysaccharides Used as Food Additives, Journal of Agricultural and Food Chemistry, vol.57, issue.15, pp.6908-6913, 2009.
DOI : 10.1021/jf900631j

M. Reynolds, M. Marradi, A. Imberty, S. Penadés, and S. Pérez, Multivalent Gold Glycoclusters: High Affinity Molecular Recognition by Bacterial Lectin PA-IL, Chemistry - A European Journal, vol.40, issue.14
DOI : 10.1107/S0021889806045833
URL : https://hal.archives-ouvertes.fr/hal-00720311

K. Marotte, C. Préville, C. Sabin, M. Moumé-pymbock, A. Imberty et al., Synthesis and binding properties of divalent and trivalent clusters of the Lewis a disaccharide moiety to Pseudomonas aeruginosa lectin PA-IIL, Organic & Biomolecular Chemistry, vol.28, issue.18, pp.2953-2961, 2007.
DOI : 10.1021/bc070129z
URL : https://hal.archives-ouvertes.fr/hal-00305549

A. Imberty and A. Varrot, Microbial recognition of human cell surface glycoconjugates, Current Opinion in Structural Biology, vol.18, issue.5, pp.567-76, 2008.
DOI : 10.1016/j.sbi.2008.08.001
URL : https://hal.archives-ouvertes.fr/hal-00352497

M. Mammen, S. Choi, and G. M. Whitesides, Polyvalent Interactions in Biological Systems: Implications for Design and Use of Multivalent Ligands and Inhibitors, Angewandte Chemie International Edition, vol.37, issue.20, pp.2754-2794, 1998.
DOI : 10.1002/(SICI)1521-3773(19981102)37:20<2754::AID-ANIE2754>3.0.CO;2-3

L. L. Kiessling, J. E. Gestwicki, and L. Strong, Synthetic multivalent ligands in the exploration of cell-surface interactions, Current Opinion in Chemical Biology, vol.4, issue.6, pp.696-703, 2000.
DOI : 10.1016/S1367-5931(00)00153-8

J. C. Sacchettini, L. G. Baum, and C. Brewer, Multivalent Protein???Carbohydrate Interactions. A New Paradigm for Supermolecular Assembly and Signal Transduction, Biochemistry, vol.40, issue.10, pp.3009-3015, 2001.
DOI : 10.1021/bi002544j

A. Goudot, Développement d'une plateforme de criblage pour la recherche de nouvelles molécules anti-infectieuses : applications à Pseudomonas aeruginosa, 2013.

S. Cecioni, S. Faure, U. Darbost, I. Bonnamour, H. Parrot-lopez et al., Selectivity among Two Lectins: Probing the Effect of Topology, Multivalency and Flexibility of ???Clicked??? Multivalent Glycoclusters, Chemistry - A European Journal, vol.11, issue.7, pp.2146-2159, 2011.
DOI : 10.1016/S0957-4166(99)00589-3
URL : https://hal.archives-ouvertes.fr/hal-00566172

S. Cecioni, R. Lalor, B. Blanchard, J. Praly, A. Imberty et al., Achieving High Affinity towards a Bacterial Lectin through Multivalent Topological Isomers of Calix[4]arene Glycoconjugates, Chemistry - A European Journal, vol.10, issue.47, pp.13232-13240, 2009.
DOI : 10.7150/ijms.5.371
URL : https://hal.archives-ouvertes.fr/hal-00691524

D. Sicard, S. Cecioni, M. Iazykov, Y. Chevolot, S. E. Matthews et al., AFM investigation of Pseudomonas aeruginosa lectin LecA (PA-IL) filaments induced by multivalent glycoclusters, Chemical Communications, vol.264, issue.33, pp.9483-9485, 2011.
DOI : 10.1016/j.febslet.2005.02.028
URL : https://hal.archives-ouvertes.fr/hal-00619415

A. Goudot, G. Pourceau, A. Meyer, T. Gehin, S. Vidal et al., Quantitative analysis (Kd and IC50) of glycoconjugates interactions with a bacterial lectin on a carbohydrate microarray with DNA Direct Immobilization (DDI), Biosensors and Bioelectronics, vol.40, issue.1, pp.153-60, 2013.
DOI : 10.1016/j.bios.2012.07.003
URL : https://hal.archives-ouvertes.fr/hal-00788052

P. Eaton and P. West, Atomic Force Microscopy, 2010.
DOI : 10.1093/acprof:oso/9780199570454.001.0001
URL : https://hal.archives-ouvertes.fr/hal-00356780

A. M. Baro, G. Ronald, and R. , Atomic Force Microscopy in Liquids, 2012.
DOI : 10.1002/9783527649808

M. B. Viani, T. E. Schäffer, A. Chand, M. Rief, H. E. Gaub et al., Small cantilevers for force spectroscopy of single molecules, Journal of Applied Physics, vol.86, issue.4, p.2258, 1999.
DOI : 10.1115/1.2874471

M. Leitner, G. E. Fantner, E. J. Fantner, K. Ivanova, T. Ivanov et al., Increased imaging speed and force sensitivity for bio-applications with small cantilevers using a conventional AFM setup, Micron, vol.43, issue.12, pp.1399-407, 2012.
DOI : 10.1016/j.micron.2012.05.007

H. J. Butt, B. Cappella, and M. Kappl, Force measurements with the atomic force microscope: Technique, interpretation and applications, Surface Science Reports, vol.59, issue.1-6, pp.1-152, 2005.
DOI : 10.1016/j.surfrep.2005.08.003

R. Lévy and M. Maaloum, Measuring the spring constant of atomic force microscope cantilevers: thermal fluctuations and other methods, Nanotechnology, vol.13, issue.1, pp.33-37, 2002.
DOI : 10.1088/0957-4484/13/1/307

J. E. Sader, J. W. Chon, and P. Mulvaney, Calibration of rectangular atomic force microscope cantilevers, Review of Scientific Instruments, vol.70, issue.10, p.3967, 1999.
DOI : 10.1063/1.1144646

J. E. Sader, J. Sanelli, B. D. Adamson, J. P. Monty, X. Wei et al., Spring constant calibration of atomic force microscope cantilevers of arbitrary shape, Review of Scientific Instruments, vol.83, issue.10, p.103705, 2012.
DOI : 10.1063/1.2140284

J. P. Cleveland, S. Manne, D. Bocek, and P. K. Hansma, A nondestructive method for determining the spring constant of cantilevers for scanning force microscopy, Review of Scientific Instruments, vol.64, issue.2, p.403, 1993.
DOI : 10.1103/PhysRevB.45.11226

A. Torii, M. Sasaki, K. Hane, and S. Okuma, A method for determining the spring constant of cantilevers for atomic force microscopy, Measurement Science and Technology, vol.7, issue.2, pp.179-184, 1999.
DOI : 10.1088/0957-0233/7/2/010

H. Butt and M. Jaschke, Calculation of thermal noise in atomic force microscopy, Nanotechnology, vol.6, issue.1, pp.1-7, 1995.
DOI : 10.1088/0957-4484/6/1/001

J. E. Sader and L. White, Theoretical analysis of the static deflection of plates for atomic force microscope applications, Journal of Applied Physics, vol.17, issue.1, p.1, 1993.
DOI : 10.1116/1.576520

C. T. Gibson, G. S. Watson, and S. Myhra, Determination of the spring constants of probes for force microscopy/spectroscopy, Nanotechnology, vol.7, issue.3, pp.259-262, 1996.
DOI : 10.1088/0957-4484/7/3/014

J. L. Hutter and J. Bechhoefer, Calibration of atomic???force microscope tips, Review of Scientific Instruments, vol.2, issue.7, p.1868, 1993.
DOI : 10.1063/1.107024

R. W. Stark, T. Drobek, and W. M. Heckl, Thermomechanical noise of a free v-shaped cantilever for atomic-force microscopy, Ultramicroscopy, vol.86, issue.1-2, pp.207-215, 2001.
DOI : 10.1016/S0304-3991(00)00077-2

B. Cappella and G. Dietler, Force-distance curves by atomic force microscopy, Surface Science Reports, vol.34, issue.1-3, pp.1-104, 1999.
DOI : 10.1016/S0167-5729(99)00003-5

H. Butt and M. Kappl, Surface and Interfacial Forces, 2010.
DOI : 10.1002/9783527629411

J. Colchero, A. Storch, M. Luna, J. Gómez-herrero, and A. M. Baró, Observation of Liquid Neck Formation with Scanning Force Microscopy Techniques, Langmuir, vol.14, issue.9, pp.2230-2234, 1998.
DOI : 10.1021/la971150z

R. Jones, H. M. Pollock, J. A. Cleaver, and C. S. Hodges, Adhesion Forces between Glass and Silicon Surfaces in Air Studied by AFM:?? Effects of Relative Humidity, Particle Size, Roughness, and Surface Treatment, Langmuir, vol.18, issue.21, pp.8045-8055, 2002.
DOI : 10.1021/la0259196

R. García and A. San-paulo, Attractive and repulsive tip-sample interaction regimes in tapping-mode atomic force microscopy, Physical Review B, vol.73, issue.7, pp.4961-4967, 1999.
DOI : 10.1063/1.122893

G. Yang, J. P. Vesenka, and C. Bustamante, Effects of tip-sample forces and humidity on the imaging of DNA with a scanning force microscope, Scanning, vol.26, issue.44, pp.344-350, 1996.
DOI : 10.1111/j.1365-2818.1994.tb03441.x

R. García and R. Pérez, Dynamic atomic force microscopy methods, Surface Science Reports, vol.47, issue.6-8, pp.197-301, 2002.
DOI : 10.1016/S0167-5729(02)00077-8

D. Leckband and J. Israelachvili, Intermolecular forces in biology, Quarterly Reviews of Biophysics, vol.34, issue.02, 2001.
DOI : 10.1017/S0033583501003687

H. J. Butt, Measuring electrostatic, van der Waals, and hydration forces in electrolyte solutions with an atomic force microscope, Biophysical Journal, vol.60, issue.6, pp.1438-1444, 1991.
DOI : 10.1016/S0006-3495(91)82180-4

D. J. Müller and . Engel, The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions, Biophysical Journal, vol.73, issue.3, pp.1633-1644, 1997.
DOI : 10.1016/S0006-3495(97)78195-5

I. D. Medalsy and D. J. Müller, Nanomechanical Properties of Proteins and Membranes Depend on Loading Rate and Electrostatic Interactions, ACS Nano, vol.7, issue.3, pp.2642-50, 2013.
DOI : 10.1021/nn400015z

C. D. Ma, C. Wang, C. Acevedo-vélez, S. H. Gellman, and N. L. Abbott, Modulation of hydrophobic interactions by proximally immobilized ions, Nature, vol.46, issue.7534, pp.347-350, 2015.
DOI : 10.1021/jp972635z

M. Rief, F. Oesterhelt, B. Heymann, and H. Gaub, Single Molecule Force Spectroscopy on Polysaccharides by Atomic Force Microscopy, Science, vol.275, issue.5304, pp.1295-1302, 1997.
DOI : 10.1126/science.275.5304.1295

C. Carrasco, M. Castellanos, P. J. Pablo, &. De, and M. G. Mateu, Manipulation of the mechanical properties of a virus by protein engineering, Proceedings of the National Academy of Sciences, vol.8, issue.1, pp.4150-4155, 2008.
DOI : 10.1016/0263-7855(90)80070-V

T. Ando, T. Uchihashi, and N. Kodera, High-Speed AFM and Applications to Biomolecular Systems, Annual Review of Biophysics, vol.42, issue.1, pp.393-414, 2013.
DOI : 10.1146/annurev-biophys-083012-130324

Y. Martin, C. C. Williams, and H. K. Wickramasinghe, Atomic force microscope???force mapping and profiling on a sub 100????? scale, Journal of Applied Physics, vol.119, issue.10, pp.4723-4729, 1987.
DOI : 10.1063/1.97288

R. Garcia, Amplitude Modulation Atomic Force Microscopy, 2010.
DOI : 10.1002/9783527632183

F. Moreno-herrero, J. Colchero, J. Gomez-herrero, and A. M. Baro, Atomic force microscopy contact, tapping, and jumping modes for imaging biological samples in liquids, Physical Review E, vol.88, issue.3, pp.1-9, 2004.
DOI : 10.1103/PhysRevLett.88.226103

S. Santos, V. Barcons, H. K. Christenson, J. Font, and N. H. Thomson, The Intrinsic Resolution Limit in the Atomic Force Microscope: Implications for Heights of Nano-Scale Features, PLoS ONE, vol.12, issue.300, pp.1-7, 2011.
DOI : 10.1371/journal.pone.0023821.s012

P. K. Hansma, J. P. Cleveland, M. Radmacher, D. A. Walters, P. E. Hillner et al., Tapping mode atomic force microscopy in liquids, Applied Physics Letters, vol.21, issue.13, pp.1738-1740, 1994.
DOI : 10.1093/nar/21.5.1117

F. Moreno-herrero, P. J. De-pablo, J. Colchero, J. Gómez-herrero, and A. M. Baró, The role of shear forces in scanning force microscopy: a comparison between the jumping mode and tapping mode, Surface Science, vol.453, issue.1-3, pp.152-158, 2000.
DOI : 10.1016/S0039-6028(00)00341-1

T. R. Albrecht, P. Grtitter, D. Horne, and D. Rugar, cantilevers for enhanced force microscope sensitivity, Journal of Applied Physics, vol.6, issue.2, pp.668-673, 1991.
DOI : 10.1063/1.104030

L. Gross, F. Mohn, N. Moll, P. Liljeroth, and G. Meyer, The Chemical Structure of a Molecule Resolved by Atomic Force Microscopy, Science, vol.27, issue.15, pp.1110-1114, 2009.
DOI : 10.1002/jcc.20495

M. J. Higgins, C. K. Riener, T. Uchihashi, J. E. Sader, R. Mckendry et al., Frequency modulation atomic force microscopy: a dynamic measurement technique for biological systems, Nanotechnology, vol.16, issue.3, pp.85-89, 2005.
DOI : 10.1088/0957-4484/16/3/016

S. Ido, K. Kimura, N. Oyabu, K. Kobayashi, M. Tsukada et al., Beyond the Helix Pitch: Direct Visualization of Native DNA in Aqueous Solution, ACS Nano, vol.7, issue.2, pp.1817-1822, 2013.
DOI : 10.1021/nn400071n

T. Ando, N. Kodera, Y. Naito, T. Kinoshita, K. Furuta et al., A High-speed Atomic Force Microscope for Studying Biological Macromolecules in Action, ChemPhysChem, vol.12, issue.11, pp.1196-1202, 2001.
DOI : 10.1016/S0960-9822(01)00683-2

F. Moreno-herrero, J. Colchero, and A. M. Baro, DNA height in scanning force microscopy, Ultramicroscopy, vol.96, issue.2, pp.167-174, 2003.
DOI : 10.1016/S0304-3991(03)00004-4

L. Martínez, M. Tello, M. Díaz, E. Román, R. Garcia et al., Aspect-ratio and lateral-resolution enhancement in force microscopy by attaching nanoclusters generated by an ion cluster source at the end of a silicon tip, Review of Scientific Instruments, vol.82, issue.2, p.23710, 2011.
DOI : 10.1103/PhysRevB.81.165430

J. S. Villarrubia, Algorithms for scanned probe microscope image simulation, surface reconstruction, and tip estimation, Journal of Research of the National Institute of Standards and Technology, vol.102, issue.4, p.425, 1997.
DOI : 10.6028/jres.102.030

H. J. Butt, M. Jaschke, and W. Ducker, Measuring surface forces in aqueous electrolyte solution with the atomic force microscope, Bioelectrochemistry and Bioenergetics, vol.38, issue.1, pp.191-201, 1995.
DOI : 10.1016/0302-4598(95)01800-T

M. E. Fuentes-perez, M. S. Dillingham, and F. Moreno-herrero, AFM volumetric methods for the characterization of proteins and nucleic acids, Methods, vol.60, issue.2, pp.113-121, 2013.
DOI : 10.1016/j.ymeth.2013.02.005

D. J. Müller and Y. Dufrêne, Atomic force microscopy: a nanoscopic window on the cell surface, Trends in Cell Biology, vol.21, issue.8, pp.461-469, 2011.
DOI : 10.1016/j.tcb.2011.04.008

P. Hinterdorfer, W. Baumgartner, H. J. Gruber, K. Schilcher, and H. Schindler, Detection and localization of individual antibody-antigen recognition events by atomic force microscopy., Proceedings of the National Academy of Sciences, vol.93, issue.8, pp.3477-81, 1996.
DOI : 10.1073/pnas.93.8.3477

P. Hinterdorfer and Y. Dufrêne, Detection and localization of single molecular recognition events using atomic force microscopy, Nature Methods, vol.34, issue.5, 2006.
DOI : 10.1042/bj1730723

S. Garcia-manyes, L. Dougan, C. L. Badilla, J. Brujic, and J. M. Fernández, Direct observation of an ensemble of stable collapsed states in the mechanical folding of ubiquitin, Proceedings of the National Academy of Sciences, vol.92, issue.8, pp.10534-10543, 2009.
DOI : 10.1529/biophysj.106.099481

M. Ludwig, M. Rief, L. Schmidt, H. Li, F. Oesterhelt et al., AFM, a tool for single-molecule experiments, Applied Physics A: Materials Science & Processing, vol.68, issue.2, pp.173-176, 1999.
DOI : 10.1007/s003390050873

J. Helenius, C. Heisenberg, H. E. Gaub, and D. J. Muller, Single-cell force spectroscopy, Journal of Cell Science, vol.121, issue.11, pp.1785-1791, 2008.
DOI : 10.1242/jcs.030999
URL : http://jcs.biologists.org/content/joces/121/11/1785.full.pdf

J. Zlatanova, S. M. Lindsay, and S. H. Leuba, Single molecule force spectroscopy in biology using the atomic force microscope, Progress in Biophysics and Molecular Biology, vol.74, issue.1-2, pp.37-61, 2000.
DOI : 10.1016/S0079-6107(00)00014-6

W. Baumgartner, P. Hinterdorfer, and H. Schindler, Data analysis of interaction forces measured with the atomic force microscope, Ultramicroscopy, vol.82, issue.1-4, pp.85-95, 2000.
DOI : 10.1016/S0304-3991(99)00154-0

G. Zoldák and M. Rief, Force as a single molecule probe of multidimensional protein energy landscapes, Current Opinion in Structural Biology, vol.23, issue.1, pp.48-57, 2013.
DOI : 10.1016/j.sbi.2012.11.007

X. Zhuang and M. Rief, Single-molecule folding, Current Opinion in Structural Biology, vol.13, issue.1, pp.88-97, 2003.
DOI : 10.1016/S0959-440X(03)00011-3

G. Francius, D. Alsteens, V. Dupres, S. Lebeer, S. De-keersmaecker et al., Stretching polysaccharides on live cells using single molecule force spectroscopy, Nature Protocols, vol.37, issue.6, pp.939-985, 2009.
DOI : 10.1007/s00249-007-0183-x

C. K. Riener, C. M. Stroh, A. Ebner, C. Klampfl, A. Gall et al., Simple test system for single molecule recognition force microscopy, Analytica Chimica Acta, vol.479, issue.1, pp.59-75, 2003.
DOI : 10.1016/S0003-2670(02)01373-9

C. Carrasco, N. S. Gilhooly, M. S. Dillingham, and F. Moreno-herrero, On the mechanism of recombination hotspot scanning during double-stranded DNA break resection, Proc. Natl
DOI : 10.1016/j.molcel.2008.03.010

C. K. Lee, Y. M. Wang, L. S. Huang, and S. Lin, Atomic force microscopy: Determination of unbinding force, off rate and energy barrier for protein???ligand interaction, Micron, vol.38, issue.5, pp.446-461, 2007.
DOI : 10.1016/j.micron.2006.06.014

H. A. Kramers, Brownian motion in a field of force and the diffusion model of chemical reactions, Physica, vol.7, issue.4, pp.284-304, 1940.
DOI : 10.1016/S0031-8914(40)90098-2

R. Merkel, P. Nassoy, R. Leung, K. Evans, and E. , Energy landscapes of receptor???ligand bonds explored with dynamic force spectroscopy, Nature, vol.394, issue.6714, pp.50-53, 1999.
DOI : 10.1038/27873

D. P. Allison, P. Hinterdorfer, and W. Han, Biomolecular force measurements and the atomic force microscope, Current Opinion in Biotechnology, vol.13, issue.1, pp.47-51, 2002.
DOI : 10.1016/S0958-1669(02)00283-5

E. Jauvert, E. Dague, M. Séverac, L. Ressier, A. Caminade et al., Probing single molecule interactions by AFM using bio-functionalized dendritips, Sensors and Actuators B: Chemical, vol.168, pp.436-441, 2012.
DOI : 10.1016/j.snb.2012.04.048
URL : https://hal.archives-ouvertes.fr/hal-01268327

A. Ebner, P. Hinterdorfer, and H. J. Gruber, Comparison of different aminofunctionalization strategies for attachment of single antibodies to AFM cantilevers, Ultramicroscopy, vol.107, issue.10-11, pp.922-929, 2007.
DOI : 10.1016/j.ultramic.2007.02.035

A. S. Kamruzzahan, A. Ebner, L. Wildling, F. Kienberger, C. K. Riener et al., Antibody Linking to Atomic Force Microscope Tips via Disulfide Bond Formation, Bioconjugate Chemistry, vol.17, issue.6, pp.1473-81, 2006.
DOI : 10.1021/bc060252a

L. Wildling, B. Unterauer, R. Zhu, A. Rupprecht, T. Haselgrübler et al., Linking of Sensor Molecules with Amino Groups to Amino-Functionalized AFM Tips, Bioconjugate Chemistry, vol.22, issue.6, pp.1239-1287, 2011.
DOI : 10.1021/bc200099t

E. Evans and K. Ritchie, Strength of a Weak Bond Connecting Flexible Polymer Chains, Biophysical Journal, vol.76, issue.5, pp.2439-2447, 1999.
DOI : 10.1016/S0006-3495(99)77399-6

Y. F. Dufrêne, Atomic Force Microscopy in Microbiology: New Structural and Functional Insights into the Microbial Cell Surface, mBio, vol.5, issue.4, pp.1-14, 2014.
DOI : 10.1128/mBio.01363-14

D. J. Muller, J. Helenius, D. Alsteens, and Y. Dufrene, Force probing surfaces of living cells to molecular resolution, Nature Chemical Biology, vol.13, issue.6, pp.383-390, 2009.
DOI : 10.1063/1.1855407

J. Friedrichs, K. R. Legate, R. Schubert, M. Bharadwaj, C. Werner et al., A practical guide to quantify cell adhesion using single-cell force spectroscopy, Methods, vol.60, issue.2, pp.169-178, 2013.
DOI : 10.1016/j.ymeth.2013.01.006

E. Sariisik, D. Docheva, D. Padula, C. Popov, J. Opfer et al., Probing the Interaction Forces of Prostate Cancer Cells with Collagen I and Bone Marrow Derived Stem Cells on the Single Cell Level, PLoS ONE, vol.32, issue.3, p.57706, 2013.
DOI : 10.1371/journal.pone.0057706.s002

M. Tulla, J. Helenius, J. Jokinen, A. Taubenberger, D. J. Müller et al., TPA primes ??2??1 integrins for cell adhesion, FEBS Letters, vol.14, issue.23-24, pp.3520-3524, 2008.
DOI : 10.1038/nm1722

M. Benoit, D. Gabriel, G. Gerisch, and H. Gaub, Discrete interactions in cell adhesion measured by single-molecule force spectroscopy, Nature Cell Biology, vol.6, issue.6, pp.313-317, 2000.
DOI : 10.1088/0957-4484/6/1/001

M. Sun, J. S. Graham, B. Hegedüs, F. Marga, Y. Zhang et al., Multiple Membrane Tethers Probed by Atomic Force Microscopy, Biophysical Journal, vol.89, issue.6, pp.4320-4329, 2005.
DOI : 10.1529/biophysj.104.058180

D. T. Le, Y. Guérardel, P. Loubire, M. Mercier-bonin, and E. Dague, Measuring Kinetic Dissociation/Association Constants Between Lactococcus lactis Bacteria and Mucins Using Living Cell Probes, Biophysical Journal, vol.101, issue.11, pp.2843-2853, 2011.
DOI : 10.1016/j.bpj.2011.10.034
URL : https://doi.org/10.1016/j.bpj.2011.10.034

E. S. Ovchinnikova, B. P. Krom, H. C. Van-der-mei, and H. J. Busscher, Force microscopic and thermodynamic analysis of the adhesion between Pseudomonas aeruginosa and Candida albicans, Soft Matter, vol.16, issue.24, p.6454, 2012.
DOI : 10.1016/S0927-7765(99)00027-2

A. Beaussart, S. El-kirat-chatel, P. Herman, D. Alsteens, J. Mahillon et al., Single-Cell Force Spectroscopy of Probiotic Bacteria, Biophysical Journal, vol.104, issue.9, pp.1886-92, 2013.
DOI : 10.1016/j.bpj.2013.03.046

V. Vadillo-rodríguez, H. J. Busscher, W. Norde, J. De-vries, R. J. Dijkstra et al., Comparison of Atomic Force Microscopy Interaction Forces between Bacteria and Silicon Nitride Substrata for Three Commonly Used Immobilization Methods, Applied and Environmental Microbiology, vol.70, issue.9, pp.5441-5446, 2004.
DOI : 10.1128/AEM.70.9.5441-5446.2004

H. Butt, B. Cappella, and M. Kappl, Force measurements with the atomic force microscope: Technique, interpretation and applications, Surface Science Reports, vol.59, issue.1-6, pp.1-152, 2005.
DOI : 10.1016/j.surfrep.2005.08.003

M. Kappl and H. J. Butt, The Colloidal Probe Technique and its Application to Adhesion Force Measurements, Particle & Particle Systems Characterization, vol.19, issue.3, pp.129-143, 2002.
DOI : 10.1002/1521-4117(200207)19:3<129::AID-PPSC129>3.0.CO;2-G

W. Ducker, T. J. Senden, and R. M. Pashley, Direct measurement of colloidal forces using an atomic force microscope, Nature, vol.353, issue.6341, pp.239-241, 1991.
DOI : 10.1038/353239a0

A. Beaussart and S. El-kirat-chatel, Quantifying the forces guiding microbial cell adhesion using single-cell force spectroscopy, Nature Protocols, vol.9, issue.5, pp.1049-55, 2014.
DOI : 10.1073/pnas.021321798

E. Kirat, K. Burton, I. Dupres, V. Dufrene, and Y. F. , Sample preparation procedures for biological atomic force microscopy, Journal of Microscopy, vol.70, issue.3, pp.199-207, 2005.
DOI : 10.1016/0014-5793(92)81241-D
URL : https://hal.archives-ouvertes.fr/hal-00017269

M. V. Maslova, L. G. Gerasimova, and W. Forsling, Surface Properties of Cleaved Mica, Colloid Journal, vol.66, issue.3, pp.322-328, 2004.
DOI : 10.1023/B:COLL.0000030843.30563.c9

A. Ebner, F. Kienberger, G. Kada, C. M. Stroh, M. Geretschläger et al., Localization of Single Avidin-Biotin Interactions Using Simultaneous Topography and Molecular Recognition Imaging, ChemPhysChem, vol.100, issue.5, pp.897-900, 2005.
DOI : 10.1016/j.ultramic.2003.12.014

H. G. Hansma and D. E. Laney, DNA binding to mica correlates with cationic radius: assay by atomic force microscopy, Biophysical Journal, vol.70, issue.4, pp.1933-1942, 1996.
DOI : 10.1016/S0006-3495(96)79757-6

M. Henger, P. Wagner, and G. Semenza, Ultralarge atomically flat template-stripped Au surfaces for scanning probe microscopy, Surf. Sci, vol.291, pp.39-46, 1993.

L. Meyer, R. Zhou, X. Tang, L. Arpanaei, A. Kingshott et al., Immobilisation of living bacteria for AFM imaging under physiological conditions, Ultramicroscopy, vol.110, issue.11, pp.1349-1357, 2010.
DOI : 10.1016/j.ultramic.2010.06.010

F. Osterhelt, M. Rief, and H. Gaub, Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water, New Journal of Physics, vol.1, pp.6-7, 1999.
DOI : 10.1088/1367-2630/1/1/006

C. Formosa, M. Grare, R. E. Duval, and E. Dague, Nanoscale effects of antibiotics on P. aeruginosa, Nanomedicine: Nanotechnology, Biology and Medicine, vol.8, issue.1, pp.12-16, 2012.
DOI : 10.1016/j.nano.2011.09.009
URL : https://hal.archives-ouvertes.fr/hal-01650395

A. Atabek and T. A. Camesano, Atomic Force Microscopy Study of the Effect of Lipopolysaccharides and Extracellular Polymers on Adhesion of Pseudomonas aeruginosa, Journal of Bacteriology, vol.189, issue.23, pp.8503-8509, 2007.
DOI : 10.1128/JB.00769-07

T. A. Camesano and N. Abu-lail, Heterogeneity in Bacterial Surface Polysaccharides, Probed on a Single-Molecule Basis, Biomacromolecules, vol.3, issue.4, pp.661-667, 2002.
DOI : 10.1021/bm015648y

A. Kannan, S. L. Karumanchi, V. Krishna, K. Thiruvengadam, S. Ramalingam et al., Nanoscale investigation on Pseudomonas aeruginosa biofilm formed on porous silicon using atomic force microscopy, Scanning, vol.36, pp.1-3, 2014.

G. Francius, S. Lebeer, D. Alsteens, L. Wildling, H. J. Gruber et al., Detection, Localization, and Conformational Analysis of Single Polysaccharide Molecules on Live Bacteria, Detection, Localization and Conformational Analysis of Single Polysaccharide Molecules on Live Bacteria, pp.1921-1929, 2008.
DOI : 10.1021/nn800341b

M. J. Waner, M. Gilchrist, M. Schindler, and M. Dantus, Imaging the Molecular Dimensions and Oligomerization of Proteins at Liquid/Solid Interfaces, The Journal of Physical Chemistry B, vol.102, issue.9, pp.1649-1657, 1998.
DOI : 10.1021/jp9732219

A. Pyne, R. Thompson, C. Leung, D. Roy, and B. W. Hoogenboom, Single-Molecule Reconstruction of Oligonucleotide Secondary Structure by Atomic Force Microscopy, Small, vol.25, issue.16, pp.3257-3261, 2014.
DOI : 10.1002/jcc.20084

N. C. Santos, M. Castanho, and R. B. , An overview of the biophysical applications of atomic force microscopy, Biophysical Chemistry, vol.107, issue.2, pp.133-149, 2004.
DOI : 10.1016/j.bpc.2003.09.001

N. Gour and S. Verma, Synthesis and AFM studies of lectin???carbohydrate self-assemblies, Tetrahedron, vol.64, issue.30-31, pp.7331-7337, 2008.
DOI : 10.1016/j.tet.2008.05.055

R. U. Kadam, D. Garg, J. Schwartz, R. Visini, M. Sattler et al., Lectin LecA, ACS Chemical Biology, vol.8, issue.9, pp.1925-1930, 2013.
DOI : 10.1021/cb400303w

D. Sicard, Y. Chevolot, E. Souteyrand, A. Imberty, S. Vidal et al., LecA (PA-IL) by atomic force microscopy: influence of the glycocluster concentration, Journal of Molecular Recognition, vol.47, issue.33, pp.694-699, 2013.
DOI : 10.1039/c1cc13097h
URL : https://hal.archives-ouvertes.fr/hal-01066774

D. Sicard, Caractérisation par microscopie à force atomique des arrangements protéine/sucre impliquant la lectine PA-IL de la bactérie pseudomonas aeruginosa, 2012.

M. Phaner-goutorbe, M. Iazykov, R. Villey, D. Sicard, and Y. Robach, Energy dissipation effects on imaging of soft materials by dynamic atomic force microscopy: A DNA-chip study, Materials Science and Engineering: C, vol.33, issue.4
DOI : 10.1016/j.msec.2013.01.055

T. K. Dam and C. Brewer, Thermodynamic Studies of Lectin???Carbohydrate Interactions by Isothermal Titration Calorimetry, Chemical Reviews, vol.102, issue.2, pp.387-429, 2002.
DOI : 10.1021/cr000401x

J. C. Martinez, J. Murciano-calles, E. S. Cobos, M. Iglesias-bexiga, I. Luque et al., in Applications of Calorimetry in a Wide Context -Differential Scanning Calorimetry, Isothermal Titration Calorimetry and Microcalorimetry, pp.73-104, 2013.

M. W. Freyer and E. Lewis, Isothermal Titration Calorimetry: Experimental Design, Data Analysis, and Probing Macromolecule/Ligand Binding and Kinetic Interactions, A. in Methods in Cell Biology, vol.84, pp.79-113, 2008.
DOI : 10.1016/S0091-679X(07)84004-0

N. Metropolis, S. Ulam, C. The-monte, and . J. Method, The Monte Carlo Method, Journal of the American Statistical Association, vol.44, issue.247, pp.335-341, 1949.
DOI : 10.1080/01621459.1949.10483310

P. Derreumaux and G. Vergoten, A new spectroscopic molecular mechanics force field. Parameters for proteins, The Journal of Chemical Physics, vol.72, issue.21, pp.8586-8605, 1995.
DOI : 10.1002/jcc.540150207

P. Lagant, D. Nolde, R. Stote, G. Vergoten, and M. Karplus, Increasing Normal Modes Analysis Accuracy:?? The SPASIBA Spectroscopic Force Field Introduced into the CHARMM Program, The Journal of Physical Chemistry A, vol.108, issue.18, pp.4019-4029, 2004.
DOI : 10.1021/jp031178l

S. Cecioni, J. P. Praly, S. E. Matthews, M. Wimmerová, A. Imberty et al., Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin-Carbohydrate Interactions: Influence of the Linker Arm, Chemistry - A European Journal, vol.36, issue.20, pp.6250-6263, 2012.
DOI : 10.1107/S0021889803021800
URL : https://hal.archives-ouvertes.fr/hal-00691472

V. Dugas, G. Depret, Y. Chevalier, X. Nesme, and É. Souteyrand, Immobilization of single-stranded DNA fragments to solid surfaces and their repeatable specific hybridization: covalent binding or adsorption?, Sensors and Actuators B: Chemical, vol.101, issue.1-2, pp.112-121, 2004.
DOI : 10.1016/j.snb.2004.02.041

M. Phaner-goutorbe, V. Dugas, Y. Chevolot, and E. Souteyrand, Silanization of silica and glass slides for DNA microarrays by impregnation and gas phase protocols: A comparative study, Materials Science and Engineering: C, vol.31, issue.2, pp.384-390, 2011.
DOI : 10.1016/j.msec.2010.10.016
URL : https://hal.archives-ouvertes.fr/hal-00877214

A. Ebner, L. Wildling, S. M. Kamruzzahan, C. Rankl, J. Wruss et al., A New, Simple Method for Linking of Antibodies to Atomic Force Microscopy Tips, Bioconjugate Chemistry, vol.18, issue.4, pp.1176-84, 2007.
DOI : 10.1021/bc070030s

H. J. Gruber, Probes Functionalization Available at

L. Dupin, F. Zuttion, T. Géhin, A. Meyer, M. Phaner-goutorbe et al., Value Determination by Using a Microarray, ChemBioChem, vol.33, issue.16, pp.2329-2336, 2015.
DOI : 10.1016/j.msec.2013.01.055
URL : https://hal.archives-ouvertes.fr/hal-01489380

P. Carl and H. Schillers, Elasticity measurement of living cells with an atomic force microscope: data acquisition and processing, Pfl??gers Archiv - European Journal of Physiology, vol.2, issue.Suppl 1, pp.551-559, 2008.
DOI : 10.1590/S0001-37652007000100003

S. Kasas, B. M. Riederer, S. Catsicas, B. Cappella, and G. Dietler, Fuzzy logic algorithm to extract specific interaction forces from atomic force microscopy data, Review of Scientific Instruments, vol.72, issue.5, pp.2082-2086, 2000.
DOI : 10.1073/pnas.90.6.2137

S. Dutta, B. A. Armitage, and Y. L. Lyubchenko, Probing of miniPEG??-PNA???DNA Hybrid Duplex Stability with AFM Force Spectroscopy, Biochemistry, vol.55, issue.10, pp.1523-1528, 2016.
DOI : 10.1021/acs.biochem.5b01250

W. Ott, M. A. Jobst, C. Schoeler, H. E. Gaub, and M. A. Nash, Single-molecule force spectroscopy on polyproteins and receptor???ligand complexes: The current toolbox, Journal of Structural Biology, vol.197, issue.1, 2016.
DOI : 10.1016/j.jsb.2016.02.011

E. Celik and V. Moy, Nonspecific interactions in AFM force spectroscopy measurements, Journal of Molecular Recognition, vol.21, issue.18, pp.53-59, 2012.
DOI : 10.1007/978-0-387-76497-9_19

S. Garde, Physical chemistry: Hydrophobic interactions in context, Nature, vol.517, issue.7534, pp.277-279, 2015.
DOI : 10.1093/protein/gzs042

A. J. Patel, P. Varilly, S. N. Jamadagni, M. F. Hagan, D. Chandler et al., Sitting at the Edge: How Biomolecules use Hydrophobicity to Tune Their Interactions and Function, The Journal of Physical Chemistry B, vol.116, issue.8, pp.2498-2503, 2012.
DOI : 10.1021/jp2107523

C. Bustamante, S. B. Smith, J. Liphardt, and D. Smith, Single-molecule studies of DNA mechanics, Current Opinion in Structural Biology, vol.10, issue.3, pp.279-85, 2000.
DOI : 10.1016/S0959-440X(00)00085-3

A. Noy and R. W. Friddle, Practical single molecule force spectroscopy: How to determine fundamental thermodynamic parameters of intermolecular bonds with an atomic force microscope, Methods, vol.60, issue.2, pp.142-50, 2013.
DOI : 10.1016/j.ymeth.2013.03.014

R. A. Copeland, D. L. Pompliano, and T. Meek, Drug???target residence time and its implications for lead optimization, Nature Reviews Drug Discovery, vol.69, issue.9, pp.730-739, 2006.
DOI : 10.1038/nrd2082

W. Dettmann, M. Grandbois, S. André, M. Benoit, A. K. Wehle et al., Differences in Zero-Force and Force-Driven Kinetics of Ligand Dissociation from ??-Galactoside-Specific Proteins (Plant and Animal Lectins, Immunoglobulin G) Monitored by Plasmon Resonance and Dynamic Single Molecule Force Microscopy, Archives of Biochemistry and Biophysics, vol.383, issue.2, pp.157-170, 2000.
DOI : 10.1006/abbi.2000.1993

T. Sulchek, R. W. Friddle, and A. Noy, Strength of Multiple Parallel Biological Bonds, Biophysical Journal, vol.90, issue.12, pp.4686-4691, 2006.
DOI : 10.1529/biophysj.105.080291

A. Beaussart, M. Abellán-flos, S. El-kirat-chatel, S. P. Vincent, and Y. Dufrêne, Force Nanoscopy as a Versatile Platform for Quantifying the Activity of Antiadhesion Compounds Targeting Bacterial Pathogens, Nano Letters, vol.16, issue.2, pp.1299-1307, 2016.
DOI : 10.1021/acs.nanolett.5b04689

K. Winzer, C. Falconer, N. C. Garber, S. P. Diggle, M. Camara et al., The Pseudomonas aeruginosa Lectins PA-IL and PA-IIL Are Controlled by Quorum Sensing and by RpoS, Journal of Bacteriology, vol.182, issue.22, pp.6401-6411, 2000.
DOI : 10.1128/JB.182.22.6401-6411.2000

A. L. Cozens, M. J. Yezzi, K. Kunzelmann, T. Ohrui, L. Chin et al., CFTR expression and chloride secretion in polarized immortal human bronchial epithelial cells., American Journal of Respiratory Cell and Molecular Biology, vol.10, issue.1, pp.38-47, 1994.
DOI : 10.1165/ajrcmb.10.1.7507342

C. Ehrhardt, C. Kneuer, J. Fiegel, J. Hanes, U. Schaefer et al., Influence of apical fluid volume on the development of functional intercellular junctions in the human epithelial cell line 16HBE14o- : implications for the use of this cell line as an in vitro model for bronchial drug absorption studies, Cell and Tissue Research, vol.308, issue.3, pp.391-400, 2002.
DOI : 10.1007/s00441-002-0548-5

H. Wan, H. L. Winton, C. Soeller, G. Stewart, P. J. Thompson et al., Tight junction properties of the immortalized human bronchial epithelial cell lines Calu???3 and 16HBE14o???, European Respiratory Journal, vol.15, issue.6, pp.1058-68, 2000.
DOI : 10.1034/j.1399-3003.2000.01514.x

R. Schubert, N. Strohmeyer, M. Bharadwaj, S. P. Ramanathan, M. Krieg et al., Assay for characterizing the recovery of vertebrate cells for adhesion measurements by single-cell force spectroscopy, FEBS Letters, vol.275, issue.19, pp.3639-3648, 2014.
DOI : 10.1074/jbc.275.7.4592

G. Ng, K. Sharma, S. M. Ward, M. D. Desrosiers, L. A. Stephens et al., Receptor-Independent, Direct Membrane Binding Leads to Cell-Surface Lipid Sorting and Syk Kinase Activation in Dendritic Cells, Receptor-Independent, Direct Membrane Binding Leads to Cell-Surface Lipid Sorting and Syk Kinase Activation in Dendritic Cells, pp.807-818, 2008.
DOI : 10.1016/j.immuni.2008.09.013

G. W. Corder and D. I. Foreman, Nonparametric Statistics. A Step-by-Step Approach, Journal of Chemical Information and Modeling, vol.53, 2014.

P. Carl, C. H. Kwok, G. Manderson, D. W. Speicher, and D. E. Discher, Forced unfolding modulated by disulfide bonds in the Ig domains of a cell adhesion molecule, Proceedings of the National Academy of Sciences, vol.220, issue.1, pp.1565-1570, 2001.
DOI : 10.1006/abio.1994.1290

S. Ostvar and B. D. Wood, Multiscale Model Describing Bacterial Adhesion and Detachment, Langmuir, vol.32, issue.20, pp.5213-5222, 2016.
DOI : 10.1021/acs.langmuir.6b00882

D. Kube, U. Sontich, D. Fletcher, and P. B. Davis, Proinflammatory cytokine responses to P. aeruginosa infection in human airway epithelial cell lines, Am.J.Physiol Lung Cell Mol.Physiol, vol.280, p.0, 2001.

A. Razatos, Y. L. Ong, M. M. Sharma, and G. Georgiou, Molecular determinants of bacterial adhesion monitored by atomic force microscopy, Proceedings of the National Academy of Sciences, vol.67, issue.2, pp.11059-11064, 1998.
DOI : 10.1016/S0006-3495(94)80556-9

T. M. Herne and M. J. Tarlov, Characterization of DNA Probes Immobilized on Gold Surfaces, Journal of the American Chemical Society, vol.119, issue.38, pp.8916-8920, 1997.
DOI : 10.1021/ja9719586

?. Doctorat and . Institut-des-nanotechnologies-de-lyon, (magali.phaner@ec-lyon.fr) Caractérisation de l'effet inhibiteur des glycomime dans l'adhésion bactérienne de P. aeruginosa par imagerie et spectroscopie (single-molecule et single-cell force spectroscopy, p.2015

C. , M. , and E. Responsable, Dr. Fernando Moreno-Herrero (fernando.moreno@cnb.csic.es) Dessin d'une cellule liquide pour l'étude de moteurs moléculaires par pince magnétique à diffèrent températures, 2010.

Y. Souteyrand, J. P. Chevolot, and . Cloarec, Nanoparticles selectively immobilized onto large arrays of gold micro and nanostructures through surface chemical functionalizations, Journal of Colloid Interface Science, vol.447, pp.152-158, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01489907

J. P. Chevolot and . Cloarec, Orthogonal chemical functionalizations of patterned gold on silica surfaces, Beilstein Journal of Nanotechnology, vol.6, pp.2272-2277, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01489429

F. Dupin, T. Zuttion, A. Gehin, M. Meyer, J. J. Phaner-goutorbe et al., Value Determination by Using a Microarray, ChemBioChem, vol.33, issue.16, pp.2329-2336, 2015.
DOI : 10.1016/j.msec.2013.01.055
URL : https://hal.archives-ouvertes.fr/hal-01489380

C. Gollnick, F. Carrasco, N. S. Zuttion, M. S. Gilhooly, F. Dillingham et al., Probing DNA Helicase Kinetics with Temperature-Controlled Magnetic Tweezers, Small, vol.348, issue.188, pp.1273-1284, 2015.
DOI : 10.1016/j.jmb.2005.03.018

M. Souteyrand and . Phaner-goutorbe, Inhibition of host-pathogen interactions in cystic fibrosis The role of lectinglycoconjugates interaction, AFM BioMed, vol.12, pp.13-17, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01489922

. Phaner-goutorbe, Inhibition of host-pathogen interaction in cystic fibrosis: a new therapeutic approach " , 18ème Journèe Scientifique du Groupe Lyonnais des Glyco-Sciences, 2015.

. Phaner-goutorbe, The cystic fibrosis pathogen Pseudomonas aeruginosa: an atomic force microscopy study for the bacterium inhibition via multivalent glycocluster " , XVI. Annual Linz Winter Workshop, pp.1-03, 2014.

M. Souteyrand and . Phaner-goutorbe, Inhibition of host-pathogen interactions in cystic fibrosis. The role of lectinglycoconjugates interaction, AFMBioMed, vol.12, pp.13-17, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01489922