Calcaripeptides A-C, cyclodepsipeptides from a Calcarisporium strain

J Nat Prod. 2013 Aug 23;76(8):1461-7. doi: 10.1021/np400262t. Epub 2013 Jul 18.

Abstract

The isolation and structure elucidation of the novel calcaripeptides A (1), B (2), and C (3) and studies on their biosynthetic origin are described. The calcaripeptides were identified from Calcarisporium sp. strain KF525, which was isolated from the German Wadden Sea. Compounds 1-3 are macrocyclic structures composed of a proline and a phenylalanine residue as well as a nonpeptidic substructure. Structure elucidation was achieved by applying one- and two-dimensional NMR spectroscopy supported by high-resolution mass spectrometry. X-ray crystallography was performed to determine the relative configuration of 1. The absolute configuration of 1 was assigned by HPLC of the amino acids after hydrolysis of the molecule and derivatization with chiral agents. Studies on the biosynthesis by feeding ¹³C-labeled substrates revealed that the nonpeptidic part of 1 originates from acetate and l-methionine. The involvement of a hybrid between a polyketide synthase and a nonribosomal peptide synthetase in the biosynthesis of the calcaripeptides is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, High Pressure Liquid
  • Crystallography, X-Ray
  • Depsipeptides / chemistry
  • Depsipeptides / isolation & purification*
  • Marine Biology
  • Methionine / metabolism
  • Mitosporic Fungi / chemistry*
  • Molecular Conformation
  • Molecular Structure
  • Nuclear Magnetic Resonance, Biomolecular
  • Oceans and Seas
  • Peptide Synthases / metabolism
  • Phenylalanine / chemistry

Substances

  • Depsipeptides
  • calcaripeptide A
  • calcaripeptide B
  • calcaripeptide C
  • Phenylalanine
  • Methionine
  • Peptide Synthases
  • non-ribosomal peptide synthase