Premium
Solution structure of an antimicrobial peptide buforin II
Author(s) -
Yi Gwan-Su,
Park Chan Bae,
Kim Sun Chang,
Cheong Chaejoon
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01193-3
Subject(s) - peptide , antimicrobial , chemistry , stereochemistry , amphiphile , antimicrobial peptides , residue (chemistry) , cationic polymerization , nuclear magnetic resonance spectroscopy , crystallography , polymer chemistry , organic chemistry , biochemistry , copolymer , polymer
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 H 2 O. In trifluoroethanol (TFE)/H 2 O (1 : 1, v/v) mixture, however, buforin II assumes a regular α‐helix between residues Val 12 and Arg 20 and a distorted helical structure between residues Gly 7 and Pro 11 . The model structure obtained shows an amphipathic character in the region from Arg 5 to the C‐terminus, Lys 21 . Like other known cationic antimicrobial peptides, the amphipathic structure might be the key factor for antimicrobial activity of buforin II.