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 Repjournal_title
BMB reportsauthors
Lee E,Jeong KW,Lee J,Shin A,Kim JK,Lee J,Lee DG,Kim Ydoi
10.5483/bmbrep.2013.46.5.252subject
Has Abstractpub_date
2013-05-01 00:00:00pages
282-7issue
5eissn
1976-6696issn
1976-670Xjournal_volume
46pub_type
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