{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sarkar S"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["2165-2178"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9526446"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(8)"],"pubmed_abstract":["The methylation of peptide backbone amides is a hallmark of bioactive natural products, and it also greatly modifies the pharmacology of synthetic peptides. Usually, bioactive <i>N</i>-methylated peptides are cyclic. However, there is very limited knowledge about how post-translational enzymes can be applied to the synthesis of designed <i>N</i>-methylated peptides or peptide libraries. Here, driven by the established ability of some RiPP enzymes to process diverse substrates, we sought to define catalysts for the <i>in vivo</i> and <i>in vitro</i> macrocyclization of backbone-methylated peptides. We developed efficient methods in which short, synthetic <i>N</i>-methylated peptides could be modified using side chain and mainchain macrocyclases, PsnB and PCY1 from plesiocin and orbitide bio"],"journal":["ACS chemical biology"],"pubmed_title":["Applying Promiscuous RiPP Enzymes to Peptide Backbone <i>N</i>-Methylation Chemistry."],"pmcid":["PMC9526446"],"funding_grant_id":["R35 GM122521","R35GM122521"],"pubmed_authors":["Sarkar S","Schmidt EW","Gu W"],"additional_accession":[]},"is_claimable":false,"name":"Applying Promiscuous RiPP Enzymes to Peptide Backbone <i>N</i>-Methylation Chemistry.","description":"The methylation of peptide backbone amides is a hallmark of bioactive natural products, and it also greatly modifies the pharmacology of synthetic peptides. Usually, bioactive <i>N</i>-methylated peptides are cyclic. However, there is very limited knowledge about how post-translational enzymes can be applied to the synthesis of designed <i>N</i>-methylated peptides or peptide libraries. Here, driven by the established ability of some RiPP enzymes to process diverse substrates, we sought to define catalysts for the <i>in vivo</i> and <i>in vitro</i> macrocyclization of backbone-methylated peptides. We developed efficient methods in which short, synthetic <i>N</i>-methylated peptides could be modified using side chain and mainchain macrocyclases, PsnB and PCY1 from plesiocin and orbitide bio","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2025-04-04T20:06:54.8Z","creation":"2025-04-04T20:06:54.8Z"},"accession":"S-EPMC9526446","cross_references":{"pubmed":["35819062"],"doi":["10.1021/acschembio.2c00293"]}}