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Quantitative Analysis of Protein Adsorption via Atomic Force Microscopy and Surface Plasmon Resonance

✍ Scribed by Eva Servoli; Devid Maniglio; Maria Rosa Aguilar; Antonella Motta; Julio San Roman; Laurence A. Belfiore; Claudio Migliaresi

Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
539 KB
Volume
8
Category
Article
ISSN
1616-5187

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✦ Synopsis

Abstract

Surface properties have a significant influence on the performance of biomedical devices. The influence of surface chemistry on the amount and distribution of adsorbed proteins has been evaluated by a combination of atomic force microscopy (AFM) and surface plasmon resonance (SPR). Adsorption of albumin, fibrinogen, and fibronectin was analyzed under static and dynamic conditions, employing self‐assembled monolayers (SAMs) as model surfaces. AFM was performed in tapping mode with antibody‐modified tips. Phase‐contrast images showed protein distribution on SAMs and phase‐shift entity provided information on protein conformation. SPR analysis revealed substrate‐specific dynamics in each system investigated. When multi‐protein solutions and diluted human plasma interacted with SAMs, SPR data suggested that surface chemistry governs the equilibrium composition of the protein layer.

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