Amino-Based Probe for Natural Products with Covalent Binding Ability to Lysine and Mechanism of Action of Medermycin

A chemoselective amino-based probe was designed for discovering natural products with covalent binding potential to lysine. Using this reactivity-based technique, a marine-derived Streptomyces strain was identified, which could produce medermycin as the major metabolite. A new compound, mederpyrrole...

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Bibliographic Details
Published in:Organic letters 2024-11, Vol.26 (47), p.10129-10134
Main Authors: Shang, Jiaxu, Yin, Shupeng, Shen, Jingjing, Gao, Chao, Wang, Weihong, Sun, Ke, Zhu, Weiming, Fu, Peng
Format: Article
Language:English
Subjects:
Biological Products - chemistry
Biological Products - metabolism
Lysine - chemistry
Molecular Structure
Naphthoquinones - chemistry
ortho-Aminobenzoates - chemistry
Pyrroles - chemistry
Pyrroles - metabolism
Streptomyces - chemistry
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Summary:A chemoselective amino-based probe was designed for discovering natural products with covalent binding potential to lysine. Using this reactivity-based technique, a marine-derived Streptomyces strain was identified, which could produce medermycin as the major metabolite. A new compound, mederpyrrole A, derived from medermycin and anthranilic acid through nonenzymatic reaction was isolated. Medermycin can react with primary amines under mild conditions to generate chimeric products possessing a naphthoquinone-pyrrole skeleton. It can also covalently bind to proteins.
ISSN:1523-7060
1523-7052
1523-7052
DOI:10.1021/acs.orglett.4c03803