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Publication Abstract from PubMed

Maximin 1 is a cationic, amphipathic antimicrobial peptide found in the skin secretions and brains of the Chinese red belly toad Bombina maxima. The 27 amino acid residue-long peptide is biologically interesting as it possesses a variety of biological activities, including antibacterial, antifungal, antiviral, antitumour and spermicidal activities. Its three-dimensional structural model was obtained in a 50/50% water/2,2,2-trifluoroethanol-d3 mixture using two-dimensional NMR spectroscopy. Maximin 1 was found to adopt an alpha-helical structure from residue Ile(2) to Ala(26) . The peptide is amphipathic, showing a clear separation between polar and non-polar residues. The interactions with sodium dodecyl sulfate micelles, a widely-used bacterial membrane-mimicking environment, were modelled using molecular dynamics simulations. The peptide maintains an alpha-helical conformation, occasionally displaying a flexibility around the Gly(9) and Gly(16) residues, which is likely responsible for the peptide's low haemolytic activity. It is found to preferentially adopt a position parallel to the micellar surface, establishing a number of hydrophobic and electrostatic interactions with the micelle.

Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1.,Timmons PB, Hewage CM J Pept Sci. 2021 Sep 26:e3370. doi: 10.1002/psc.3370. PMID:34569121^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.