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Purification and Modeling Amphipathic Alpha Helical Antimicrobial Peptides from Skin Secretions of E uphlyctis cyanophlyctis
Author(s) -
Asoodeh Ahmad,
Sepahi Samaneh,
GhoraniAzam Adel
Publication year - 2014
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.12256
Subject(s) - antimicrobial , antimicrobial peptides , bacillus cereus , staphylococcus aureus , microbiology and biotechnology , antibacterial activity , bacteria , escherichia coli , klebsiella pneumoniae , chemistry , gram positive bacteria , biology , peptide , gram negative bacteria , biochemistry , genetics , gene
Antimicrobial peptides as ancient immune system are found in almost all types of living organisms. Amphibian's skin is an important source of bioactive peptides with strong antibacterial, antiviral, and antitumor properties. They have important role in inducing apoptosis as well as cancer therapy in vitro . In this study, we extracted and purified antimicrobial peptides from skin secretions of Euphlyctis cyanophlyctis and named them brevinin‐Eu and cyanophlyctin β . They showed favorable antibacterial properties on both Gram‐positive and Gram‐negative bacteria with ignorable hemolytic activity of <1.9% and 0.7% at very high concentrations of brevinin‐Eu and cyanophlyctin β , respectively. For antibacterial activity and MIC determination, two Gram‐positive ( Staphylococcus aureus PTCC 1431 and B. cereus PTCC 1247) and two Gram‐negative bacteria ( Escherichia coli HP 101 BA 7601c and Klebsiella pneumoniae PTCC 1388) were assayed. MIC values of extracted peptides demonstrated that they can inhibit bacterial growth at very low concentration (17 and 12 μ g/mL) for brevinin‐Eu and cyanophlyctin β , respectively. Structural prediction suggested that the brevinin‐Eu can efficiently bind and destroy bacterial membrane, but cyanophlyctin β uses a diverse mode of action.