Talaropeptides A-D: Structure and Biosynthesis of Extensively N-methylated Linear Peptides From an Australian Marine Tunicate-Derived Talaromyces sp.

Frontiers in Chemistry

Esteban Marcellin¹  Zeinab G. Khalil²  Pradeep Dewapriya²  Angela A. Salim²  Robert J. Capon²  Pritesh Prasad²  Pablo Cruz-Morales³ 

[1]Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, QLD, Australia

[2]Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD, Australia

[3]Joint BioEnergy Institute, Emeryville, CA, United States

关键词: marine-derived;    fungus;    Talaromyces;    talaropeptide;    NRPS;    linear peptide;   

DOI  :  10.3389/fchem.2018.00394

来源: DOAJ

【 摘 要 】

An Australian marine tunicate-derived fungus, Talaromyces sp. CMB-TU011 was subjected to a program of analytical microbioreactor (MATRIX) cultivations, supported by UHPLC-QTOF profiling, to reveal conditions for producing a new class of extensively N-methylated 11-12 residue linear peptides, talaropeptides A-D (2-5). The structures for 2-5, inclusive of absolute configurations, were determined by a combination of detailed spectroscopic and chemical (e.g., C3 and C18 Marfey's) analyses. We report on the biological properties of 2-5, including plasma stability, as well as antibacterial, antifungal and cell cytotoxicity. The talaropeptide mega non-ribosomal peptide synthetase (NRPS) is described, as second only in size to that for the fungus-derived immunosuppressant cyclosporine (an 11-residue extensively N-methylated cyclic peptide).

【 授权许可】

Unknown