Influence of Solvent in Controlling Peptide-Surface Interactions

Daniel A. Cannon, Nurit Ashkenasy, Tell Tuttle

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Protein binding to surfaces is an important phenomenon in biology and in modern technological applications. Extensive experimental and theoretical research has been focused in recent years on revealing the factors that govern binding affinity to surfaces. Theoretical studies mainly focus on examining the contribution of the individual amino acids or, alternatively, the binding potential energies of the full peptide, which are unable to capture entropic contributions and neglect the dynamic nature of the system. We present here a methodology that involves the combination of nonequilibrium dynamics simulations with strategic mutation of polar residues to reveal the different factors governing the binding free energy of a peptide to a surface. Using a gold-binding peptide as an example, we show that relative binding free energies are a consequence of the balance between strong interactions of the peptide with the surface and the ability for the bulk solvent to stabilize the peptide.

Original languageEnglish
Pages (from-to)3944-3949
Number of pages6
JournalJournal of Physical Chemistry Letters
Issue number19
StatePublished - 1 Oct 2015


  • binding free energy
  • peptide-surface
  • solvent stabilization
  • steered molecular dynamics
  • surface binding

ASJC Scopus subject areas

  • Materials Science (all)
  • Physical and Theoretical Chemistry


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