Publication:
Effect of N-terminal truncation on antibacterial activity, cytotoxicity and membrane perturbation activity of Cc-CATH3

dc.contributor.authorJiraphun Jittikoonen_US
dc.contributor.authorNarumon Ngamsaithongen_US
dc.contributor.authorJutarat Pimthonen_US
dc.contributor.authorOpa Vajraguptaen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-11-23T09:37:39Z
dc.date.available2018-11-23T09:37:39Z
dc.date.issued2015-10-01en_US
dc.description.abstract© 2015 The Pharmaceutical Society of Korea. A series of amino-terminal truncated analogues of quail antimicrobial peptide Cc-CATH3(1-29) were created and examined antibacterial activity against Gram-positive bacteria, cytotoxicity against mouse fibroblast cell line, and membrane perturbation activity against various membrane models. Parent peptide Cc-CATH3(1-29) and the first four-residue truncated peptide Cc-CATH3(5-29) were active in all tested experiments. In contrast, the eight- and twelve-residue truncated variants Cc-CATH3(9-29) and Cc-CATH3(13-29) appeared to have lost activities. Cc-CATH3(1-29) and Cc-CATH3(5-29) possessed antibacterial activity with minimum inhibitory concentrations of 2-4 and 1-2 μM, respectively. For cytotoxicity, Cc-CATH3(1-29) and Cc-CATH3(5-29) displayed cytotoxicity with the IC50 values of 9.33 and 4.93 μM, respectively. Cc-CATH3(5-29) induced greater liposome membranes disruption than Cc-CATH3(1-29) regardless of lipid type and composition. The leakage results of Cc-CATH3(1-29) share a similar trend with that in Cc-CATH3(5-29); they exhibit no preferential binding to anionic phospholipids. In conclusion, the results suggested that the first four residues at the N-terminus "RVRR" is not essential for presenting all test activities. In contrast, residues five to eight of "FWPL" are necessary as the exclusion of this short motif in Cc-CATH3(9-29) and Cc-CATH3(13-29) leads to a loss of activities. This study will be beneficial for further design and development of Cc-CATH3 to be novel antibiotic.en_US
dc.identifier.citationArchives of Pharmacal Research. Vol.38, No.10 (2015), 1839-1849en_US
dc.identifier.doi10.1007/s12272-015-0600-0en_US
dc.identifier.issn19763786en_US
dc.identifier.issn02536269en_US
dc.identifier.other2-s2.0-84944150230en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/123456789/35366
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84944150230&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemistryen_US
dc.titleEffect of N-terminal truncation on antibacterial activity, cytotoxicity and membrane perturbation activity of Cc-CATH3en_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84944150230&origin=inwarden_US
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