7OVZ

SOLUTION NMR STRUCTURE OF MAXIMIN 1 IN 50% TRIFLUOROETHANOL

Summary for 7OVZ

• Entry DOI: 10.2210/pdb7ovz/pdb
• Related: 6HZ2
• NMR Information: BMRB: 34639
• Descriptor: Maximin-1 (1 entity in total)
• Functional Keywords: maximin 1, antimicrobial peptide, antimicrobial protein
• Biological source: Bombina maxima (Giant fire-bellied toad, Chinese red belly toad)
• Total number of polymer chains: 1
• Total formula weight: 2679.16

Authors

Timmons, P.B.,Hewage, C.M. (deposition date: 2021-06-15, release date: 2021-10-13, Last modification date: 2024-06-19)

Primary citation

Timmons, P.B.,Hewage, C.M.
Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1.
J.Pept.Sci., 28:e3370-e3370, 2022

PubMed Abstract: 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-d mixture using two-dimensional NMR spectroscopy. Maximin 1 was found to adopt an α-helical structure from residue Ile to Ala . 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 α-helical conformation, occasionally displaying a flexibility around the Gly and Gly 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.

PubMed: 34569121
DOI: 10.1002/psc.3370

Experimental method

SOLUTION NMR