Salt effects on surface-tethered peptides in solution

Jun Feng, Ka Yiu Wong, Gillian C. Lynch, Xiaolian Gao, B. Montgomery Pettitt

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


The capability to manipulate proteins/peptide fragments at liquid-solid interfaces has led to tremendous applications in detectors and biotechnology. Therefore, understanding the detailed molecular behavior of proteins and peptides tethered on a hard material surface is an interesting and important topic. The inhomogeneity presented by surfaces as well as ions in the solution plays an important role in the thermodynamics and kinetics of the tethered proteins. In this study, we perform a series of molecular dynamics simulations of a pentapeptide RHSVV, a p53 epitope, tethered on a prepared microarray surface in various salt concentrations (0, 0.14, 0.5, and 1 M NaCl), as well as free in ionic solution (0, 0.5, and 1 M). The conformational space the tethered peptide visits largely overlaps with the free peptide in solution. However, surface tethering as well as the salt concentration changes both the thermodynamics and kinetics of the peptide. Frequent conformational changes are observed during the simulations and tend to be slowed down by both increasing the salt concentration and surface tethering. The local composition of ions at different salt concentrations is also compared between the tethered and free peptide.

Original languageEnglish (US)
Pages (from-to)9472-9478
Number of pages7
JournalJournal of Physical Chemistry B
Issue number28
StatePublished - Jul 16 2009
Externally publishedYes

ASJC Scopus subject areas

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


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