Cyclic heptapeptides with metal binding properties isolated from the fungus Cadophora malorum from Antarctic soil

Abstract The Antarctic fungus Cadophora malorum produces previously undescribed cyclic heptapeptides (cadophorin A and B) containing an anthranilic acid residue. The planar structure of these peptides was determined by high-resolution mass spectrometry combined with extensive 1D and 2D NMR spectrosc...

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Bibliographic Details
Published in:Natural Products and Bioprospecting
Main Authors: Guidmar C. Donalle, María Martha Martorell, Gastón E. Siless, Lucas Ruberto, Gabriela M. Cabrera
Format: Article in Journal/Newspaper
Language:English
Published: SpringerOpen 2022
Subjects:
Cyclic peptide
Cadophora malorum
Metal binding
Botany
QK1-989
Allo
Antarctic
The Antarctic
Antarc*
Online Access:https://doi.org/10.1007/s13659-022-00348-x
https://doaj.org/article/a4f73dc546944d0b89984a23cdbfee29
Description
Summary:Abstract The Antarctic fungus Cadophora malorum produces previously undescribed cyclic heptapeptides (cadophorin A and B) containing an anthranilic acid residue. The planar structure of these peptides was determined by high-resolution mass spectrometry combined with extensive 1D and 2D NMR spectroscopy. The absolute configuration of the amino acids was determined by Marfey’s method, with HPLC analysis of FDVA (Nα-(2,4-dinitro-5-fluorphenyl)-l-valinamide) derivatives making use of a PFP column. Remarkably, cadophorin 2 possesses both the uncommon d-Ile and d-allo-Ile in its structure. The peptides have metal binding properties as shown by LCMS with post column addition of metal salt solutions. These results were supported by DFT calculations. Graphical Abstract

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