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

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...

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Bibliographic Details
Published in:Natural Products and Bioprospecting
Main Authors: Donalle, Guidmar C., Martorell, María Martha, Siless, Gastón E., Ruberto, Lucas, Cabrera, Gabriela M.
Format: Text
Language:English
Published: Springer Nature Singapore 2022
Subjects:
Original Article
Allo
Antarctic
The Antarctic
Antarc*
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9279517/
http://www.ncbi.nlm.nih.gov/pubmed/35831516
https://doi.org/10.1007/s13659-022-00348-x
Description
Summary: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: [Image: see text] SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s13659-022-00348-x.

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