We have chosen a sixteen residue polyglycine peptide model to study the effect of Hydrophobic interfaces on the conformational equilibria of peptide backbones. Owing to the absence of sidechain residues, Polyglycine serves as a useful model to study generic polypeptide backbones. We have performed extensive molecular dynamics simulations using state-of-the-art forcefields to study the behavior of polyglycine in bulk and near a Hydrophobic interface. The Hydrophobic interface has been modeled through a Self-Assembled monolayer (SAM) surface that has been modeled using two surfactant chains each comprising C10 alkane chains with -CH3 head group at one end attached to sulfur atoms whose positions are fixed in space. We observe that at 300K, polyglycine remains adsorbed near the surface of the SAM. Interestingly we observe significant propensity of beta-sheets stabilized by intra-peptide hydrogen bonds near the SAM surface. These results highlight the modulation of intrinsic preferences of peptide backbones near hydrophobic surfaces.

How do hydrophobic surfaces modulate the conformational equilibria of protein backbones?

256th National Meeting (2018)

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