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

A chemoselective\namino-based probe was designed for discovering\nnatural products with covalent binding potential to lysine. Using\nthis reactivity-based technique, a marine-derived Streptomyces strain was identified, which could produce medermycin as the major\nmetabolite. A new compound, mederpyrrole A, derived from medermycin\nand anthranilic acid through nonenzymatic reaction was isolated. Medermycin\ncan react with primary amines under mild conditions to generate chimeric\nproducts possessing a naphthoquinone-pyrrole skeleton. It can also\ncovalently bind to proteins.

Publication Details

Journal
Figshare
Published
2024-11-19
DOI
https://doi.org/10.1021/acs.orglett.4c03803.s001
Primary Topic
Supramolecular Chemistry and Complexes
Type
article
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0.00
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article

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

Figshare
Supramolecular Chemistry and Complexes
article

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

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Abstract

A chemoselective\namino-based probe was designed for discovering\nnatural products with covalent binding potential to lysine. Using\nthis reactivity-based technique, a marine-derived Streptomyces strain was identified, which could produce medermycin as the major\nmetabolite. A new compound, mederpyrrole A, derived from medermycin\nand anthranilic acid through nonenzymatic reaction was isolated. Medermycin\ncan react with primary amines under mild conditions to generate chimeric\nproducts possessing a naphthoquinone-pyrrole skeleton. It can also\ncovalently bind to proteins.

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Supramolecular Chemistry and Complexes
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Amino-Based Probe for Natural Products with Covalent\nBinding Ability to Lysine and Mechanism of Action of Medermycin · Figshare (2024) | TGRS Research Map | TGRS