STRUCTURE, FUNCTION, AND MEMBRANE INTEGRATION OF DEFENSINS

Citation
Sh. White et al., STRUCTURE, FUNCTION, AND MEMBRANE INTEGRATION OF DEFENSINS, Current opinion in structural biology, 5(4), 1995, pp. 521-527
Citations number
43
Categorie Soggetti
Cell Biology",Biology
ISSN journal
0959440X
Volume
5
Issue
4
Year of publication
1995
Pages
521 - 527
Database
ISI
SICI code
0959-440X(1995)5:4<521:SFAMIO>2.0.ZU;2-M
Abstract
Defensins comprise a structural class of small cationic peptides that exert broad-spectrum antimicrobial activities through membrane permeab ilization. Their predominantly beta-sheet structure, stabilized by thr ee disulfide bonds, distinguishes them from other antimicrobial peptid es which typically form amphiphilic helices. Defensins bind to membran es electrostatically and subsequently form apparently multimeric pores . Recent structural and biophysical studies are beginning to provide i nsights into the process of permeabilization.