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Crystal Structure of Heymonin, a Novel Frog-derived PeptideCrystal Structure of Heymonin, a Novel Frog-derived Peptide
Structural highlights
Publication Abstract from PubMedAntimicrobial peptides form part of the innate immune response and play a vital role in host defense against pathogens. Here we report a new antimicrobial peptide belonging to the cathelicidin family, cathelicidin-MH (cath-MH), from the skin of Microhyla heymonsivogt frog. Cath-MH has a single alpha-helical structure in membrane-mimetic environments and is antimicrobial against fungi and bacteria, especially Gram-negative bacteria. In contrast to other cathelicidins, cath-MH suppresses coagulation by affecting the enzymatic activities of tissue plasminogen activator, plasmin, beta-tryptase, elastase, thrombin, and chymase. Cath-MH protects against lipopolysaccharide (LPS)- and cecal ligation and puncture-induced sepsis, effectively ameliorating multiorgan pathology and inflammatory cytokine through its antimicrobial, LPS-neutralizing, coagulation suppressing effects as well as suppression of MAPK signaling. Taken together, these data suggest that cath-MH is an attractive candidate therapeutic agent for the treatment of septic shock. Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties.,Chai J, Chen X, Ye T, Zeng B, Zeng Q, Wu J, Kascakova B, Martins LA, Prudnikova T, Smatanova IK, Kotsyfakis M, Xu X Elife. 2021 Apr 20;10. pii: 64411. doi: 10.7554/eLife.64411. PMID:33875135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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