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A theoretical analysis of the thermodynamic contributions for the adsorption of individual protein residues on functionalized surfaces

Paper ID Volume ID Publish Year Pages File Format Full-Text
13098 829 2002 16 PDF Available
Title
A theoretical analysis of the thermodynamic contributions for the adsorption of individual protein residues on functionalized surfaces
Abstract

Although the denaturing of adsorbed proteins on biomaterials surfaces is believed to lead to adverse tissue reactions to implanted materials, very little is currently known of the actual mechanisms involved. These mechanisms must be understood if surfaces are to be proactively designed to control protein adsorption behavior. Concepts widely employed in rational drug design and in protein and RNA folding predictions provide a means to approach this problem. Accordingly, a theoretical analysis has been conducted to estimate the thermodynamic contributions (changes in enthalpy, entropy, and Gibbs free energy) for the adsorption of selected individual mid-chain protein residues to functionalized surfaces. Enthalpic contributions from residue–surface interactions were calculated using semi-empirical quantum mechanical-based computational chemistry methods in a simulated aqueous environment (MOPAC/COSMO), and enthalpic and entropic contributions due to water restructuring effects assumed to occur during adsorption were estimated from experimental data for functional group wetting and calculated changes in solvent accessible surface area as each protein residue approached each surface. When combined with intraprotein residue–residue interactions, the understanding of residue–surface adsorption energy relationships provides a means to begin to predict protein adsorption behavior as a function of biomaterials surface chemistry. It is recognized that several assumptions have been made in this approach that could be challenged, and that truncations necessary due to programming limitations have been applied that may neglect potentially important interactions. Therefore, it must be understood that the modeling predictions may not be directly applicable to biomaterials for surface design under actual physiologic conditions at this stage. However, this attempt at modeling fundamental components of protein adsorption is presented as an initial approach to understanding these complex events.

Keywords
Protein adsorption; Thermodynamics; Enthalpy; Entropy; Gibbs free energy; Self-assembled monolayers
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A theoretical analysis of the thermodynamic contributions for the adsorption of individual protein residues on functionalized surfaces
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 23, Issue 23, December 2002, Pages 4633–4648
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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