Structure-activity relationships of cecropin-like peptides and their interactions with phospholipid membrane.

Abstract:

:Cecropin A and papiliocin are novel 37-residue cecropin-like antimicrobial peptides isolated from insect. We have confirmed that papiliocin possess high bacterial cell selectivity and has an α-helical structure from Lys(3) to Lys(21) and from Ala(25) to Val(35), linked by a hinge region. In this study, we demonstrated that both peptides showed high antimicrobial activities against multi-drug resistant Gram negative bacteria as well as fungi. Interactions between these cecropin-like peptides and phospholipid membrane were studied using CD, dye leakage experiments, and NMR experiments, showing that both peptides have strong permeabilizing activities against bacterial cell membranes and fungal membranes as well as Trp(2) and Phe(5) at the N-terminal helix play an important role in attracting cecropin-like peptides to the negatively charged bacterial cell membrane. Cecropin-like peptides can be potent peptide antibiotics against multi-drug resistant Gram negative bacteria and fungi.

journal_name

BMB Rep

journal_title

BMB reports

authors

Lee E,Jeong KW,Lee J,Shin A,Kim JK,Lee J,Lee DG,Kim Y

doi

10.5483/bmbrep.2013.46.5.252

subject

Has Abstract

pub_date

2013-05-01 00:00:00

pages

282-7

issue

5

eissn

1976-6696

issn

1976-670X

journal_volume

46

pub_type

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