Structural and conformational analysis of hydroxycyclochlorotine and cyclochlorotine, chlorinated cyclic peptides from Penicillium islandicum

J Nat Prod. 2008 Jul;71(7):1297-300. doi: 10.1021/np800150m. Epub 2008 Jun 18.

Abstract

A new chlorinated cyclic pentapeptide, hydroxycyclochlorotine (1), has been isolated from Penicillium islandicum, and the structure including absolute stereochemistry of 1 and conformational properties of 1 and cyclochlorotine (2) in DMSO-d6 were elucidated by using extensive 2D NMR and chemical means. Hydroxycyclochlorotine (1) and astin B (3) from Aster tataricus, each containing an allo threonine at residue 2, have a cis proline configuration, whereas cyclochlorotine (2) has two conformational states in solution, which may be produced from cis-trans isomerization of the proline amide bond. The presence of an intramolecular hydrogen bond between Ser (3)-NH and a hydroxyl oxygen atom of alloThr (2) may serve to maintain the backbone conformation with a cis proline amide bond.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Molecular Structure
  • Penicillium / chemistry*
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / isolation & purification*

Substances

  • Peptides, Cyclic
  • astin B
  • hydroxycyclochlorotine