Hierarchical self-assembly in diblock copolypeptides of poly(γ-benzyl-l-glutamate) with poly poly(l-leucine) and poly(O-benzyl-l-tyrosine)

M. Mondeshki, H. W. Spiess, T. Aliferis, H. Iatrou, Nikolaos Hadjichristidis, G. Floudas*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Block copolypeptides with their inherent nanometer length scale of phase separation, provide means of manipulating the type (α-helices, β-strands) and persistence of peptide secondary structures. Two such examples are employed based on the α-helical poly(γ-benzyl-l- glutamate) (PBLG) polypeptide as one block and poly(l-leucine) (α-helical) or poly(O-benzyl-l-tyrosine) (POBT) (β-strands) as the second block. Although both secondary structures are present in the copolypeptides the effect of nano-scale confinement is to induce folding in the POBT β-sheets and to maintain the defected α-helices of PBLG and PLEU with a limited lateral coherence.

Original languageEnglish (US)
Pages (from-to)668-674
Number of pages7
JournalEuropean Polymer Journal
Volume47
Issue number4
DOIs
StatePublished - Apr 1 2011

Keywords

  • Copolypeptides
  • Self-assembly
  • α-Helices
  • β-Strands

ASJC Scopus subject areas

  • Polymers and Plastics
  • Physics and Astronomy(all)
  • Organic Chemistry

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