Publication:
Antibacterial potential of a novel peptide from the consensus sequence of dermaseptin related peptides secreted by agalychnis annae

dc.contributor.authorYa’U Sabo Ajingien_US
dc.contributor.authorAuwal Muhammaden_US
dc.contributor.authorPongsak Khunraeen_US
dc.contributor.authorTriwit Rattanarojpongen_US
dc.contributor.authorKovit Pattanapanyasaten_US
dc.contributor.authorThana Sutthibutpongen_US
dc.contributor.authorNujarin Jongrujaen_US
dc.contributor.otherSiriraj Hospitalen_US
dc.contributor.otherKano University of Science and Technologyen_US
dc.contributor.otherKing Mongkut's University of Technology Thonburien_US
dc.date.accessioned2022-08-04T08:13:50Z
dc.date.available2022-08-04T08:13:50Z
dc.date.issued2021-01-01en_US
dc.description.abstractBackground: The consistently increasing reports of bacterial resistance and the reemergence of bacterial epidemics have inspired the health and scientific community to discover new molecules with antibacterial potential continuously. Frog-skin secretions constitute bioactive compounds essential for finding new biopharmaceuticals. The exact antibacterial characterization of dermaseptin related peptides derived from Agalychnis annae, is limited. The resemblance in their conserved and functionally linked genomes indicates an unprecedented opportunity to obtain novel bioactive compounds. Objective: In this study, we derived a novel peptide sequence and determined its antibacterial potentials. Methods: Consensus sequence strategy was used to design the novel and active antibacterial peptide named 'AGAAN' from skin secretions of Agalychnis annae. The in-vitro activities of the novel peptide against some bacterial strains were investigated. Time kill studies, DNA retardation, cytotoxicity, betagalactosidase, and molecular computational studies were conducted. Results: AGAAN inhibited P. aeruginosa, E. faecalis, and S. typhimurium at 20 µM concentration. E. coli and S. aureus were inhibited at 25 µM, and lastly, B. subtilis at 50 µM. Kinetics of inactivation against exponential and stationary growing bacteria was found to be rapid within 1-5 hours of peptide exposure, depending on time and concentration. The peptide displayed weak hemolytic activity between 0.01%-7.31% at the antibacterial concentrations. AGAAN efficiently induced bacterial membrane damage with subsequent cell lysis. The peptide's DNA binding shows that it also targets intracellular DNA by retarding its movement. Our in-silico molecular docking analysis displayed a strong affinity to the bacterial cytoplasmic membrane. Conclusion: AGAAN exhibits potential antibacterial properties that could be used to combat bacterial resistance.en_US
dc.identifier.citationCurrent Pharmaceutical Biotechnology. Vol.22, No.9 (2021), 1216-1227en_US
dc.identifier.doi10.2174/1389201021666201020161428en_US
dc.identifier.issn18734316en_US
dc.identifier.issn13892010en_US
dc.identifier.other2-s2.0-85112119673en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/76350
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85112119673&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectPharmacology, Toxicology and Pharmaceuticsen_US
dc.titleAntibacterial potential of a novel peptide from the consensus sequence of dermaseptin related peptides secreted by agalychnis annaeen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85112119673&origin=inwarden_US

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