Structure and mechanism for iterative amide N -methylation in the biosynthesis of channel-forming peptide cytotoxins | Zendy

D.P. Cogan | Zendy; Agneya Bhushan | Zendy; Reyvin M. Reyes | Zendy; Lingyang Zhu | Zendy; Jörn Piel | Zendy; Satish K. Nair | Zendy

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Structure and mechanism for iterative amide N -methylation in the biosynthesis of channel-forming peptide cytotoxins

Author(s) -

D.P. Cogan,

Agneya Bhushan,

Reyvin M. Reyes,

Lingyang Zhu,

Jörn Piel,

Satish K. Nair

Publication year - 2022

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.2116578119

Subject(s) - biosynthesis , methylation , mechanism (biology) , peptide , amide , chemistry , cytotoxicity , channel (broadcasting) , biochemistry , microbiology and biotechnology , computational biology , stereochemistry , biology , gene , computer science , in vitro , philosophy , computer network , epistemology

Significance The channel-forming proteusins are bacterial helical peptides that allow permeation of positively charged ions to influence membrane potential and cellular physiology. We biochemically characterize the effect of two critical posttranslational modifications on the secondary structure of the peptide substrate. We determine how a methyl group can be added to the side chains of D-Asn residues in a peptide substrate and show how flanking residues influence selectivity. These studies should foster the development of small-molecule peptide ion channels as therapeutics.

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