{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zheng Y"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["14006-14014"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9928189"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(22)"],"pubmed_abstract":["<i>N</i>-methylation of peptide backbones has often been utilized as a strategy towards the development of peptidic drugs. However, difficulties in the chemical synthesis, high cost of enantiopure <i>N</i>-methyl building blocks, and subsequent coupling inefficiencies have hampered larger-scale medicinal chemical efforts. Here, we present a chemoenzymatic strategy for backbone <i>N</i>-methylation by bioconjugation of peptides of interest to the catalytic scaffold of a borosin-type methyltransferase. Crystal structures of a substrate tolerant enzyme from <i>Mycena rosella</i> guided the design of a decoupled catalytic scaffold that can be linked via a heterobifunctional crosslinker to any peptide substrate of choice. Peptides linked to the scaffold, including those with non-proteinogenic r"],"journal":["ACS catalysis"],"pubmed_title":["Bioconjugate Platform for Iterative Backbone <i>N</i>-Methylation of Peptides."],"pmcid":["PMC9928189"],"funding_grant_id":["R01 GM131347","R01 GM079038"],"pubmed_authors":["Zheng Y","Ongpipattanakul C","Nair SK"],"additional_accession":[]},"is_claimable":false,"name":"Bioconjugate Platform for Iterative Backbone <i>N</i>-Methylation of Peptides.","description":"<i>N</i>-methylation of peptide backbones has often been utilized as a strategy towards the development of peptidic drugs. However, difficulties in the chemical synthesis, high cost of enantiopure <i>N</i>-methyl building blocks, and subsequent coupling inefficiencies have hampered larger-scale medicinal chemical efforts. Here, we present a chemoenzymatic strategy for backbone <i>N</i>-methylation by bioconjugation of peptides of interest to the catalytic scaffold of a borosin-type methyltransferase. Crystal structures of a substrate tolerant enzyme from <i>Mycena rosella</i> guided the design of a decoupled catalytic scaffold that can be linked via a heterobifunctional crosslinker to any peptide substrate of choice. Peptides linked to the scaffold, including those with non-proteinogenic r","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-28T11:29:15.83Z","creation":"2025-02-19T03:27:05.857Z"},"accession":"S-EPMC9928189","cross_references":{"pubmed":["36793448"],"doi":["10.1021/acscatal.2c04681"]}}