Characterizing the Switching Transitions of an Adsorbed Peptide by Mapping the Potential Energy Surface

James A. Ross-Naylor, Milan Mijajlovic, Hu Zhang, Mark J. Biggs

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Peptide adsorption occurs across technology, medicine, and nature. The functions of adsorbed peptides are related to their conformation. In the past, molecular simulation methods such as molecular dynamics have been used to determine key conformations of adsorbed peptides. However, the transitions between these conformations often occur too slowly to be modeled reliably by such methods. This means such transitions are less well understood. In the study reported here, discrete path sampling is used for the first time to study the potential energy surface of an adsorbed peptide (polyalanine) and the transition pathways between various stable adsorbed conformations that have been identified in prior work by two of the authors [ Mijajlovic, M.; Biggs, M. J. J. Phys. Chem. C 2007, 111, 15839-15847 ]. Mechanisms for the switching of adsorbed polyalanine between the stable conformations are elucidated along with the energetics of these switches.

Original languageEnglish
Pages (from-to)11455-11464
Number of pages10
JournalJournal of Physical Chemistry B
Volume121
Issue number51
Early online date19 Dec 2017
DOIs
Publication statusPublished - 28 Dec 2017

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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