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|Title: ||Molecular-level understanding of protein adsorption at the interface between water and a strongly interacting uncharged solid surface|
|Authors: ||Penna, M.J.|
Biggs, Mark J.
|Issue Date: ||2014|
|Publisher: ||© American Chemical Society (ACS)|
|Citation: ||PENNA, M.J., MIJAJLOVIC, M. and BIGGS, M.J., 2014. Molecular-level understanding of protein adsorption at the interface between water and a strongly interacting uncharged solid surface. Journal of the American Chemical Society, 136 (14), pp. 5323-5331.|
|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. © 2014 American Chemical Society.|
|Description: ||This paper is published in Journal of the American Chemical Society and the definitive version can be found at https://doi.org/10.1021/ja411796e.s001. Its reuse is subject to the ACS terms and conditions http://pubs.acs.org/page/policy/authorchoice_termsofuse.html The supplementary information is available via the link below.|
|Publisher Link: ||http://dx.doi.org/10.1021/ja411796e|
|Related Resource: ||https://doi.org/10.1021/ja411796e.s001|
|Appears in Collections:||Published Articles (Chemistry)|
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