6HZ2

SOLUTION NMR STRUCTURE OF MAXIMIN 3 IN 50% TRIFLUOROETHANOL

Summary for 6HZ2

• Entry DOI: 10.2210/pdb6hz2/pdb
• NMR Information: BMRB: 34322
• Descriptor: Maximins 3/H11 type 2 (1 entity in total)
• Functional Keywords: maximin 3 antimicrobial peptide alpha helix, antimicrobial protein
• Biological source: Bombina maxima (Giant fire-bellied toad)
• Total number of polymer chains: 1
• Total formula weight: 2703.21

Authors

Benetti, S.,Timmons, P.B.,Hewage, C.M. (deposition date: 2018-10-22, release date: 2019-02-20, Last modification date: 2024-06-19)

Primary citation

Benetti, S.,Timmons, P.B.,Hewage, C.M.
NMR model structure of the antimicrobial peptide maximin 3.
Eur.Biophys.J., 48:203-212, 2019

PubMed Abstract: Maximin 3 is a 27-residue-long cationic antimicrobial peptide found in the skin secretion and brain of the Chinese red-belly toad Bombina maxima. The peptide is of biological interest as it possesses anti-HIV activity, not found in the other maximin peptides, in addition to antimicrobial, antitumor and spermicidal activities. The three-dimensional structure of maximin 3 was obtained in a 50/50% water/2,2,2-trifluoroethanol-d mixture using two-dimensional NMR spectroscopy. Maximin 3 was found to adopt an α-helical structure from residue G1 to A22, and a coil structure with a helical propensity in the C-terminal tail. The peptide is amphipathic, showing a clear separation between polar and hydrophobic residues. Interactions with sodium dodecyl sulfate micelles, a widely used bacterial membrane-mimicking environment, were modeled using molecular dynamics simulations. The peptide maintained an α-helical conformation, occasionally displaying a flexibility around residues G9 and G16, 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 it.

PubMed: 30734844
DOI: 10.1007/s00249-019-01346-7

Experimental method

SOLUTION NMR