Factors governing helix formation in peptides confined to carbon nanotubes

Edward P. O'Brien, George Stan, D. Thirumalai, Bernard R. Brooks

Research output: Contribution to journalArticle

33 Scopus citations

Abstract

The effect of confinement on the stability and dynamics of peptides and proteins is relevant in the context of a number of problems in biology and biotechnology. We have examined the stability of different helix-forming sequences upon confinement to a carbon nanotube using Langevin dynamics simulations of a coarse-grained representation of the polypeptide chain. We show that the interplay of several factors that include sequence, solvent conditions, strength (λ) of nanotube-peptide interactions, and the nanotube diameter (D) determines confinement-induced stability of helicies. In agreement with predictions based on polymer theory, the helical state is entropically stabilized for all sequences when the interaction between the peptide and the nanotube is weakly hydrophobic and D is small. However, there is a strong sequence dependence as the strength of the λ increases. For an amphiphilic sequence, the helical stability increases with λ, whereas for polyalanine the diagram of states is a complex function of λ and D. In addition, decreasing the size of the "hydrophobic patch" lining the nanotube, which mimics the chemical heterogeneity of the ribosome tunnel, increases the helical stability of the polyalanine sequence. Our results provide a framework for interpreting a number of experiments involving the structure formation of peptides in the ribosome tunnel as well as transport of biopolymers through nanotubes.

Original languageEnglish (US)
Pages (from-to)3702-3708
Number of pages7
JournalNano letters
Volume8
Issue number11
DOIs
StatePublished - Nov 1 2008

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All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Chemistry(all)
  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanical Engineering

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