Simple jQuery Dropdowns
Please use this identifier to cite or link to this item:
Title: Characterization of the novel antibacterial peptide Leucrocin from crocodile (Crocodylus siamensis) white blood cell extracts
Authors: Supawadee Pata
Nualyai Yaraksa
Sakda Daduang
Yosapong Temsiripong
Jisnuson Svasti
Tomohiro Araki
Sompong Thammasirirak
Khon Kaen University
Sriracha Moda Co.
Mahidol University
Tokai University
Keywords: Biochemistry, Genetics and Molecular Biology;Immunology and Microbiology
Issue Date: 1-May-2011
Citation: Developmental and Comparative Immunology. Vol.35, No.5 (2011), 545-553
Abstract: Four novel antibacterial peptides, Leucrocin I-IV from Siamese crocodile white blood cell extracts were purified by reverse phase high performance liquid chromatography (RP-HPLC). Leucrocins exhibit strong antibacterial activity towards Staphylococcus epidermidis, Salmonella typhi and Vibrio cholerae. The peptides were 7-10 residues in length with different primary structure. The amino acid sequence of Leucrocin I is NGVQPKY with molecular mass around 806.99. Da and Leucrocin II is NAGSLLSGWG with molecular mass around 956.3. Da. Further, the interaction between peptides and bacterial membranes as part of their killing mechanism was studied by fluorescence and electron microscopy. The outer membrane and cytoplasmic membrane was the target of action of Leucrocins as assayed in model membrane by release of β-galactosidase due to the membrane permeabilization. Finally, the hemolytic effect was tested against human red blood cell. Leucrocin I, III and IV showed less toxicity against human red blood cells than Leucrocin II. © 2010 Elsevier Ltd.
ISSN: 0145305X
Appears in Collections:Scopus 2011-2015

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.