New design of helix bundle peptide-polymer conjugates

Biomacromolecules. 2008 Aug;9(8):2111-7. doi: 10.1021/bm800113g. Epub 2008 Jul 16.

Abstract

We present a new design of peptide-polymer conjugates where a polymer chain is covalently linked to the side chain of a helix bundle-forming peptide. The effect of conjugated polymer chains on the peptide structure was examined using a de novo designed three-helix bundle and a photoactive four-helix bundle. Upon attachment of poly(ethylene glycol) to the exterior of the coiled-coil helix bundle, the peptide secondary structure was stabilized and the tertiary structure, that is, the coiled-coil helix bundle, was retained. When a heme-binding peptide as an example is used, the new peptide-polymer conjugate architecture also preserves the built-in functionalities within the interior of the helix bundle. It is expected that the conjugated polymer chains act to mediate the interactions between the helix bundle and its external environment. Thus, this new peptide-polymer conjugate design strategy may open new avenues to macroscopically assemble the helix bundles and may enable them to function in nonbiological environments.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biocompatible Materials / chemistry*
  • Chromatography, High Pressure Liquid
  • Circular Dichroism
  • Hydrogen-Ion Concentration
  • Molecular Conformation
  • Peptides / chemistry*
  • Polyethylene Glycols / chemistry
  • Polymers / chemistry*
  • Protein Folding
  • Protein Structure, Secondary
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Spectrophotometry, Ultraviolet / methods
  • Ultracentrifugation

Substances

  • Biocompatible Materials
  • Peptides
  • Polymers
  • Polyethylene Glycols