{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cabalteja CC"],"funding":["Division of Chemistry","National Institute of Allergy and Infectious Diseases","NIAID NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["987-997"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9039985"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(4)"],"pubmed_abstract":["The emergence of resistance to clinically used antibiotics by bacteria presents a significant problem in public health. Natural antimicrobial peptides (AMPs) are a valuable source of antibiotics that act by a mechanism less prone to the evolutionary development of resistance. In an effort to realize the promise of AMPs while overcoming limitations such as poor biostability, researchers have sought sequence-defined oligomers with artificial amide-based backbones that show membrane-disrupting functions similar to natural agents. Most of this precedent has focused on short peptidomimetic analogues of unstructured chains or secondary folds; however, the natural antimicrobial arsenal includes a number of small- and medium-sized proteins that act via an ordered tertiary structure. Generating pro"],"journal":["ACS chemical biology"],"pubmed_title":["Heterogeneous-Backbone Proteomimetic Analogues of Lasiocepsin, a Disulfide-Rich Antimicrobial Peptide with a Compact Tertiary Fold."],"pmcid":["PMC9039985"],"funding_grant_id":["CHE 1625002","AI133351","GM107161","R01 GM107161","R01 AI133351"],"pubmed_authors":["Lin Q","Harmon TW","Cabalteja CC","Horne WS","Rao SR","Di YP"],"additional_accession":[]},"is_claimable":false,"name":"Heterogeneous-Backbone Proteomimetic Analogues of Lasiocepsin, a Disulfide-Rich Antimicrobial Peptide with a Compact Tertiary Fold.","description":"The emergence of resistance to clinically used antibiotics by bacteria presents a significant problem in public health. Natural antimicrobial peptides (AMPs) are a valuable source of antibiotics that act by a mechanism less prone to the evolutionary development of resistance. In an effort to realize the promise of AMPs while overcoming limitations such as poor biostability, researchers have sought sequence-defined oligomers with artificial amide-based backbones that show membrane-disrupting functions similar to natural agents. Most of this precedent has focused on short peptidomimetic analogues of unstructured chains or secondary folds; however, the natural antimicrobial arsenal includes a number of small- and medium-sized proteins that act via an ordered tertiary structure. Generating pro","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-05-09T22:22:45.421Z","creation":"2025-02-19T04:46:16.535Z"},"accession":"S-EPMC9039985","cross_references":{"pubmed":["35290019"],"doi":["10.1021/acschembio.2c00138"]}}