Solution structure of an antimicrobial peptide buforin II

FEBS Letters
G S YiChaejoon Cheong

Abstract

The structure of 21-residue antimicrobial peptide buforin II has been determined by using NMR spectroscopy and restrained molecular dynamics. Buforin II adopts a flexible random structure in H2O. In trifluoroethanol (TFE)/H2O (1:1, v/v) mixture, however, buforin II assumes a regular alpha-helix between residues Val12 and Arg20 and a distorted helical structure between residues Gly7 and Pro11. The model structure obtained shows an amphipathic character in the region from Arg5 to the C-terminus, Lys21. Like other known cationic antimicrobial peptides, the amphipathic structure might be the key factor for antimicrobial activity of buforin II.

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Citations

May 20, 1999·Biopolymers·D Andreu, L Rivas
Aug 10, 2000·Biopolymers·A TossiA Giangaspero
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Oct 7, 2021·Biochemistry·Nils PreußkeFrank D Sönnichsen

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