| Literature DB >> 24192554 |
Nualyai Yaraksa1, Thitiporn Anunthawan1, Tinnakorn Theansungnoen1, Sakda Daduang1, Tomohiro Araki2, Apisak Dhiravisit3, Sompong Thammasirirak1.
Abstract
Leucrocin I is an antibacterial peptide isolated from crocodile (Crocodylus siamensis) white blood cell extracts. Based on Leucrocin I sequence, cationic peptide, NY15, was designed, synthesized and evaluated for antibacterial activity against Bacillus sphaericus TISTR 678, Bacillus megaterium (clinical isolate), Vibrio cholerae (clinical isolate), Salmonella typhi (clinical isolate), Salmonella typhi ATCC 5784 and Escherichia coli 0157:H7. The efficacy of the peptide made from all L-amino acids was also compared with all D-amino acids. The peptide made from all D-amino acids was more active than the corresponding L-enantiomer. In our detailed study, the interaction between peptides and the cell membrane of Vibrio cholerae as part of their killing mechanism was studied by fluorescence and electron microscopy. The results show that the membrane was the target of action of the peptides. Finally, the cytotoxicity assays revealed that both L-NY15 and D-NY15 peptides are non-toxic to mammalian cells at bacteriolytic concentrations.Entities:
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Year: 2013 PMID: 24192554 DOI: 10.1038/ja.2013.114
Source DB: PubMed Journal: J Antibiot (Tokyo) ISSN: 0021-8820 Impact factor: 2.649