{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bello-Madruga R"],"funding":["a node of the Spanish Large-Scale National Facility","Ministerio de Ciencia e Innovación (MCIN)","NMR experiments were performed in the “Manuel Rico” NMR laboratory (LMR) of the Spanish National Research Council","Ministerio de Ciencia e Innovación","the Departament de Recerca i Universitats de la Generalitat de Catalunya","European Society of Clinical Microbiology and Infectious Diseases","'la Caixa' Foundation ('la Caixa')","European Society of Clinical Microbiology and Infectious Diseases (ESCMID)","'la Caixa' Foundation"],"pagination":["889-910"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12223310"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(7)"],"pubmed_abstract":["Glycosaminoglycan (GAG)-binding proteins regulating essential processes such as cell growth and migration are essential for cell homeostasis. As both GAGs and the lipid A disaccharide core of Gram-negative bacteria contain negatively charged disaccharide units, we hypothesized that GAG-binding proteins could also recognize LPS and enclose cryptic antibiotic motifs. Here, we report novel antimicrobial peptides (AMPs) derived from heparin-binding proteins (HBPs), with specific activity against Gram-negative bacteria and high LPS binding. We used computational tools to locate antimicrobial regions in 82% of HBPs, most of those colocalizing with putative heparin-binding sites. To validate these results, we synthesized five candidates [HBP-1-5] that showed remarkable activity against Gram-negat"],"journal":["Molecular systems biology"],"pubmed_title":["Mining the heparinome for cryptic antimicrobial peptides that selectively kill Gram-negative bacteria."],"pmcid":["PMC12223310"],"funding_grant_id":["ESCMID2022","PID2020-113184RB-C22","PRTR-C17.I1","PDC2021-121544-I00 funded by MCIN/AEI /10.13039/501100011033 and European Union Next GenerationEU/ P","HR17-00409","PRE2021-097678","María de Maeztu network of Units of Excellence","PRE2018-083243","PID2020-112821GB-I00 funded by MCIN/AEI /10.13039/501100011033","PID2020-114627RB-I00 funded by MCIN/AEI /10.13039/501100011033","2023PROD00021"],"pubmed_authors":["Gomez J","Bello-Madruga R","Torrent M","Valle J","Comas L","Gonzalez-Lopez JJ","Jimenez MA","Sandin D","Larrosa MN","Andreu D"],"additional_accession":[]},"is_claimable":false,"name":"Mining the heparinome for cryptic antimicrobial peptides that selectively kill Gram-negative bacteria.","description":"Glycosaminoglycan (GAG)-binding proteins regulating essential processes such as cell growth and migration are essential for cell homeostasis. As both GAGs and the lipid A disaccharide core of Gram-negative bacteria contain negatively charged disaccharide units, we hypothesized that GAG-binding proteins could also recognize LPS and enclose cryptic antibiotic motifs. Here, we report novel antimicrobial peptides (AMPs) derived from heparin-binding proteins (HBPs), with specific activity against Gram-negative bacteria and high LPS binding. We used computational tools to locate antimicrobial regions in 82% of HBPs, most of those colocalizing with putative heparin-binding sites. To validate these results, we synthesized five candidates [HBP-1-5] that showed remarkable activity against Gram-negat","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jul","modification":"2026-06-03T01:43:23.393Z","creation":"2026-05-28T03:05:21.801Z"},"accession":"S-EPMC12223310","cross_references":{"pubmed":["40410382"],"doi":["10.1038/s44320-025-00120-6"]}}