Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/91092
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Type: Journal article
Title: Molecular-level understanding of protein adsorption at the interface between water and a strongly interacting uncharged solid surface
Author: Penna, M.
Mijajlovic, M.
Biggs, M.
Citation: Journal of the American Chemical Society, 2014; 136(14):5323-5331
Publisher: American Chemical Society
Issue Date: 2014
ISSN: 0002-7863
1520-5126
Statement of
Responsibility: 
Matthew J. Penna, Milan Mijajlovic, and Mark J. Biggs
Abstract: Although protein adsorption on solids is of immense relevance, experimental limitations mean there is still a remarkable lack of understanding of the adsorption mechanism, particularly at a molecular level. By subjecting 240+ molecular dynamics simulations of two peptide/water/solid surface systems to statistical analysis, a generalized molecular level mechanism for peptide adsorption has been identified for uncharged surfaces that interact strongly with the solution phase. This mechanism is composed of three phases: (1) biased diffusion of the peptide from the bulk phase toward the surface; (2) anchoring of the peptide to the water/solid interface via interaction of a hydrophilic group with the water adjacent to the surface or a strongly interacting hydrophobic group with the surface; and (3) lockdown of the peptide on the surface via a slow, stepwise and largely sequential adsorption of its residues, which we term 'statistical zippering'. The adsorption mechanism is dictated by the existence of water layers adjacent to the solid and orientational ordering therein. By extending the solid into the solution by ~8 Å and endowing it with a charged character, the water layers ensure the peptide feels the effect of the solid at a range well beyond the dispersion force that arises from it, thus inducing biased diffusion from afar. The charging of the interface also facilitates anchoring of the peptide near the surface via one of its hydrophilic groups, allowing it time it would otherwise not have to rearrange and lockdown. Finally, the slowness of the lockdown process is dictated by the need for the peptide groups to replace adjacent tightly bound interfacial water.
Keywords: Graphite
Water
Proteins
Diffusion
Protein Conformation
Adsorption
Surface Properties
Molecular Dynamics Simulation
Hydrophobic and Hydrophilic Interactions
Description: Publication Date (Web): February 7, 2014
Rights: © 2014 American Chemical Society
DOI: 10.1021/ja411796e
Appears in Collections:Aurora harvest 7
Chemical Engineering publications

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