Structure and mechanism for iterative amide <i>N</i>-methylation in the biosynthesis of channel-forming peptide cytotoxins.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 35316135.
- Also identified by DOI 10.1073/pnas.2116578119 and PMC identifier 9060474.
- Licence recorded as CC BY-NC-ND.
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Abstract
SignificanceThe 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.
Medical subject headings
- Amides
- Cytotoxins