{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Muhammad T"],"funding":["Elisabeth and Alfred Ahlqvists stiftelse","Swedish Research Council","Elisabeth and Alfred Ahlqvists stiftelse postdoctoral scholarship"],"pagination":["504"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9953701"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(2)"],"pubmed_abstract":["Is it possible to enhance structural stability and biological activity of KR-12, a truncated antimicrobial peptide derived from the human host defense peptide LL-37? Based on the mapping of essential residues in KR-12, we have designed backbone-cyclized dimers, cross-linked via a disulfide bond to improve peptide stability, while at the same time improving on-target activity. Circular dichroism showed that each of the dimers adopts a primarily alpha-helical conformation (55% helical content) when bound to lyso-phosphatidylglycerol micelles, indicating that the helical propensity of the parent peptide is maintained in the new cross-linked cyclic form. Compared to KR-12, one of the cross-linked dimers showed 16-fold more potent antimicrobial activity against human pathogens <i>Pseudomonas ae"],"journal":["Biomedicines"],"pubmed_title":["Transforming Cross-Linked Cyclic Dimers of KR-12 into Stable and Potent Antimicrobial Drug Leads."],"pmcid":["PMC9953701"],"funding_grant_id":["Medicine and Health, #2011-03403; UG","Postdoctoral Scholarship: TM","#2011-03403"],"pubmed_authors":["Gunasekera S","Muhammad T","Stromstedt AA","Goransson U"],"additional_accession":[]},"is_claimable":false,"name":"Transforming Cross-Linked Cyclic Dimers of KR-12 into Stable and Potent Antimicrobial Drug Leads.","description":"Is it possible to enhance structural stability and biological activity of KR-12, a truncated antimicrobial peptide derived from the human host defense peptide LL-37? Based on the mapping of essential residues in KR-12, we have designed backbone-cyclized dimers, cross-linked via a disulfide bond to improve peptide stability, while at the same time improving on-target activity. Circular dichroism showed that each of the dimers adopts a primarily alpha-helical conformation (55% helical content) when bound to lyso-phosphatidylglycerol micelles, indicating that the helical propensity of the parent peptide is maintained in the new cross-linked cyclic form. Compared to KR-12, one of the cross-linked dimers showed 16-fold more potent antimicrobial activity against human pathogens <i>Pseudomonas ae","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2026-04-08T14:33:04.234Z","creation":"2025-02-18T23:44:22.418Z"},"accession":"S-EPMC9953701","cross_references":{"pubmed":["36831040"],"doi":["10.3390/biomedicines11020504"]}}