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• W3015008266 abstract "A growing number of evidence shows that human-associated microbiota is an important contributor in health and disease. However, much of the complexity of host-microbiota interaction remains to be elucidated both at cellular and molecular levels. Siderophores are chemically diverse, ferric-specific chelators synthesized and secreted by microbes to secure their iron acquisition. The host defense peptide LL-37 is ubiquitously produced at epithelial surfaces modulating microbial communities and suppressing pathogenic strains. The present work demonstrates that LL-37 binds tightly siderocalin-resistant stealth siderophores which are important contributors to the virulence of several pathogens. As indicated by circular dichroism spectroscopic experiments, addition of aerobactin and rhizoferrin increases the membrane active α-helical conformation of the partially folded peptide. The cationic nature of LL-37 (+6 net charge at pH 7.4) and the multiple carboxylate groups present in siderophores refer to the dominant contribution of electrostatic interactions in the stabilization of peptide-chelator adducts. It is proposed that aside siderocalin proteins, LL-37 may be a complementary, less specific component of the siderophore scavenging repertoire of the innate immune system." @default.
• W3015008266 created "2020-04-10" @default.
• W3015008266 creator A5023886494 @default.
• W3015008266 creator A5055019777 @default.
• W3015008266 date "2020-06-01" @default.
• W3015008266 modified "2023-10-07" @default.
• W3015008266 title "Human host-defense peptide LL-37 targets stealth siderophores" @default.
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• W3015008266 doi "https://doi.org/10.1016/j.bbrc.2020.03.162" @default.
• W3015008266 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32265033" @default.
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