Control of peptide secondary structure and dynamics in poly(γ-benzyl- L-glutamate)-b-polyalanine peptides

A. Gitsas, G. Floudas*, M. Mondeshki, H. W. Spiess, T. Aliferis, H. Iatrou, N. Hadjichristidis

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

The stability, persistence and dynamics of the peptide secondary motifs are investigated in a series of poly(γ-benzyl-L-glutamate)-b-polyalanine (PBLG-b-PAla) polypeptides through a combination of structural (X-rays, NMR) and dynamic (Dielectric Spectroscopy, NMR) probes. The unfavorable enthalpic interactions between the unlike blocks give rise to nanophase separation that results in the destabilization of PAla β-sheets. Contrary to this, the overall helicity of PBLG α-helices is enhanced. The dynamics of the "defected" amorphous segments and of the more ordered segments are studied by DS and 13C NMR, respectively. These probes provide information on the time scale and the mechanism of molecular and supramolecular motion.

Original languageEnglish (US)
Pages (from-to)8072-8080
Number of pages9
JournalMacromolecules
Volume41
Issue number21
DOIs
StatePublished - Nov 11 2008
Externally publishedYes

ASJC Scopus subject areas

  • Organic Chemistry
  • Materials Chemistry
  • Polymers and Plastics
  • Inorganic Chemistry

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