Cyclic α,β-tetrapeptoids: sequence-dependent cyclization and conformational preference

Org Lett. 2013 Jul 19;15(14):3626-9. doi: 10.1021/ol401478j. Epub 2013 Jun 27.

Abstract

The presence of at least one N-Cα branched side chain is crucial for successful cyclization of α,β-tetrapeptoids. The ctct amide sequence revealed in the crystal structure of the 14-membered cyclotetrapeptoid 8 is also the most populated conformation in solution and is reminiscent of the predominant amide arrangement of the 12-membered cyclic tetrapeptides (CTPs).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Crystallography, X-Ray
  • Cyclization
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Conformation
  • Oligopeptides / chemistry*
  • Peptoids / chemistry*

Substances

  • Oligopeptides
  • Peptoids