{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9"],"submitter":["Spassov DS"],"pubmed_abstract":["The salt bridge is the strongest non-covalent interaction in nature and is known to participate in protein folding, protein-protein interactions, and molecular recognition. However, the role of salt bridges in the context of drug design has remained not well understood. Here, we report that a common feature in the mechanism of inhibition of the N-myristoyltransferases (NMT), promising targets for the treatment of protozoan infections and cancer, is the formation of a salt bridge between a positively charged chemical group of the small molecule and the negatively charged C-terminus of the enzyme. Substituting the inhibitor positively charged amine group with a neutral methylene group prevents the formation of the salt bridge and leads to a dramatic activity loss. Molecular dynamics simulati"],"journal":["Frontiers in molecular biosciences"],"pagination":["1066029"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9871453"],"repository":["biostudies-literature"],"pubmed_title":["A role of salt bridges in mediating drug potency: A lesson from the N-myristoyltransferase inhibitors."],"pmcid":["PMC9871453"],"pubmed_authors":["Atanasova M","Doytchinova I","Spassov DS"],"additional_accession":[]},"is_claimable":false,"name":"A role of salt bridges in mediating drug potency: A lesson from the N-myristoyltransferase inhibitors.","description":"The salt bridge is the strongest non-covalent interaction in nature and is known to participate in protein folding, protein-protein interactions, and molecular recognition. However, the role of salt bridges in the context of drug design has remained not well understood. Here, we report that a common feature in the mechanism of inhibition of the N-myristoyltransferases (NMT), promising targets for the treatment of protozoan infections and cancer, is the formation of a salt bridge between a positively charged chemical group of the small molecule and the negatively charged C-terminus of the enzyme. Substituting the inhibitor positively charged amine group with a neutral methylene group prevents the formation of the salt bridge and leads to a dramatic activity loss. Molecular dynamics simulati","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-26T13:15:15.046Z","creation":"2024-11-20T11:06:53.395Z"},"accession":"S-EPMC9871453","cross_references":{"pubmed":["36703920"],"doi":["10.3389/fmolb.2022.1066029"]}}