Direct Measurement of Protein Adhesion at Biomaterial Surfaces by Scanning Force Microscopy

Vansteenkiste, Stefan; Corneillie, Siska; Schacht, Etienne; Chen, X; Davies, Martyn C.; Moens, Maurice; Vaeck, Luc Van

doi:10.1021/la981740c

Cited by 33 publications

(23 citation statements)

References 42 publications

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“…9 The invention and the widespread of the use of atomic force microscopy ͑AFM͒ initiated further a series of direct and accurate measurements of the interaction forces between modified tips and surfaces [10][11][12][13][14][15] and this technique was soon exploited for the study of the influence of pH and ionic strength on the interaction between adsorbed protein layers. [16][17][18][19] Atomic force spectroscopy is based on recording the deflection of a very sensitive cantilever, while it is approaching or being retracted from a surface.…”

Section: Introductionmentioning

confidence: 99%

Measurement of interaction forces between fibrinogen coated probes and mica surface with the atomic force microscope: The pH and ionic strength effect

Tsapikouni¹,

Allen²,

Missirlis³

2008

Biointerphases

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The study of protein-surface interactions is of great significance in the design of biomaterials and the evaluation of molecular processes in tissue engineering. The authors have used atomic force microscopy (AFM) to directly measure the force of attraction/adhesion of fibrinogen coated tips to mica surfaces and reveal the effect of the surrounding solution pH and ionic strength on this interaction. Silica colloid spheres were attached to the AFM cantilevers and, after plasma deposition of poly(acrylic acid), fibrinogen molecules were covalently bound on them with the help of the cross-linker 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) in the presence of N-hydroxysulfosuccinimide (sulfo-NHS(. The measurements suggest that fibrinogen adsorption is controlled by the screening of electrostatic repulsion as the salt concentration increases from 15 to 150 mM, whereas at higher ionic strength (500 mM) the hydration forces and the compact molecular conformation become crucial, restricting adsorption. The protein attraction to the surface increases at the isoelectric point of fibrinogen (pH 5.8), compared with the physiological pH. At pH 3.5, apart from fibrinogen attraction to the surface, evidence of fibrinogen conformational changes is observed, as the pH and the ionic strength are set back and forth, and these changes may account for fibrinogen aggregation in the protein solution at this pH.

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Section: Introductionmentioning

confidence: 99%

Measurement of interaction forces between fibrinogen coated probes and mica surface with the atomic force microscope: The pH and ionic strength effect

Tsapikouni¹,

Allen²,

Missirlis³

2008

Biointerphases

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“…In contrast, hydrophobic surfaces, such as octadecyltrichlorosilane SAMs, tend to adsorb proteins as a monolayer thick biofilm (25,26,27). The current understanding of the difference in protein adhesion is related to the interfacial free energy of the coating in water (surface hydrophobicity), steric repulsion of the functionalized surface against protein (entropy losses in chain conformation and solvent expulsion), and conformational changes allowed by the adsorbing protein (28,29,30).…”

Section: Introductionmentioning

confidence: 99%

Protein Adhesion on SAM Coated Semiconductor Wafers: Hydrophobic versus Hydrophilic Surfaces

Follstaedt¹,

Cheung²,

Gourley³

et al. 2000

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The interface of biology and semiconductor materials has become an important topic of interest as researchers are merging living organisms with microelectromechanical systems (MEMS) in the pursuit of new microfabricated biomedical devices. Biological cells interface with the semiconductor surface through a host of interactions that are mediated by protein adhesion and film formation. To better understand this interface, we have conducted protein adsorption studies of a model system using bovine serum albumin (BSA) and compared it to the adsorption from a complex protein mixture of cell growth serum on uncoated and self-assembled monolayer (SAM) coated silicon wafers. Several characterization techniques -AFM, ellipsometry, water contact angle, and fluorescence microscopy -were used to evaluate the protein-adsorbed layer. An uncoated silicon surface was most attractive to proteins, forming a 70 Å thick film from a solution of BSA at a concentration comparable to that in cell growth serum. Coating with the hydrophobic octadecyltrimethoxysilane (OTMS) SAM reduced protein adhesion by ~15%. In contrast, a hydrophilic N-(triethoxysilylpropyl)-O-polyethyleneoxide urethane (TESP) SAM inhibited protein adhesion by greater than 50%. Protein adhesion studies with cell growth sera containing complex mixtures of proteins paralleled the BSA adsorption studies, clearly identifying the TESP coated surface as a promising biocompatible coating.4

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“…21,22 The principles of AFM as a molecular force probe have been described in detail. 15 -19,23,24 As the AFM tip approaches and contacts the surface, there is generally a measurable adhesive response as the tip is retracted, owing to interaction forces between the tip and the surface.…”

mentioning

confidence: 99%

Molecular Interactions Between a Plant Virus Movement Protein and RNA: Force Spectroscopy Investigation

Андреев¹,

Kim²,

Калинина

et al. 2004

Journal of Molecular Biology

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Direct Measurement of Protein Adhesion at Biomaterial Surfaces by Scanning Force Microscopy

Cited by 33 publications

References 42 publications

Measurement of interaction forces between fibrinogen coated probes and mica surface with the atomic force microscope: The pH and ionic strength effect

Measurement of interaction forces between fibrinogen coated probes and mica surface with the atomic force microscope: The pH and ionic strength effect

Protein Adhesion on SAM Coated Semiconductor Wafers: Hydrophobic versus Hydrophilic Surfaces

Molecular Interactions Between a Plant Virus Movement Protein and RNA: Force Spectroscopy Investigation

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