Interplay between adsorbed peptide structure, trapped water, and surface hydrophobicity

Biointerphases
Katherine D KrauseDennis K Hore

Abstract

Atomistic molecular dynamics simulations were used to study the influence of interfacial water on the orientation and conformation of a facewise amphipathic α-helical peptide adsorbed to hydrophilic and hydrophobic substrates. Water behavior beneath the peptide adsorbed to a hydrophilic surface was observed to vary with the height of the peptide above the surface. In general, the orientation of water close to the peptide (with the oxygen atom pointing up toward the peptide) was complementary to that observed near the hydrophilic surface in the absence of peptide. That is, no change in orientation of water trapped between the peptide and a hydrophilic surface is required as the peptide approaches the surface. The adsorption of the peptide to the hydrophilic surface was observed to be mediated by a layer of ordered water. Water was found to be largely excluded on adsorption to the hydrophobic surface. However, the small amount of water present was observed to be highly ordered. At the closest point of contact to the hydrophobic surface, the peptide was observed to make direct contact. These findings shed light on the fundamental driving forces of peptide adsorption to hydrophobic and hydrophilic surfaces in aqueous environments.

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Citations

Jan 30, 2020·Biomaterials Science·Haifeng Fan, Zhiguang Guo
Jul 1, 2017·Biointerphases·Tobias Weidner
Jul 14, 2021·The Journal of Physical Chemistry. B·Wen GuoZhan Chen
Aug 29, 2018·Accounts of Chemical Research·Tasha JariszDennis K Hore
Mar 14, 2019·Langmuir : the ACS Journal of Surfaces and Colloids·Grazia M L MessinaGiovanni Marletta

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