Macrocyclic design strategies for small, stable parallel beta-sheet scaffolds

J Am Chem Soc. 2009 Jun 17;131(23):7970-2. doi: 10.1021/ja902210f.

Abstract

Pairs of short peptide strands can be induced to adopt an antiparallel beta-sheet secondary structure in aqueous solution via a macrocyclic constraint, as illustrated by many natural and designed peptides. We show that an analogous strategy is successful for creation of small units of parallel beta-sheet secondary structure in aqueous solution. Cyclization in this case requires nonpeptide segments for N-to-N and C-to-C interstrand linkage. Surprisingly, we find that only one of these segments needs to be preorganized.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Cyclization
  • Peptides / chemical synthesis*
  • Peptides / chemistry
  • Protein Structure, Secondary*

Substances

  • Peptides