{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,30]],"date-time":"2025-10-30T11:37:52Z","timestamp":1761824272931,"version":"3.40.5"},"reference-count":80,"publisher":"Bentham Science Publishers Ltd.","issue":"9","content-domain":{"domain":["eurekaselect.com"],"crossmark-restriction":true},"short-container-title":["CPB"],"published-print":{"date-parts":[[2021,7]]},"abstract":"<jats:sec><jats:title>Background:<\/jats:title><jats:p>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.<\/jats:p><\/jats:sec><jats:sec><jats:title>Objective:<\/jats:title><jats:p>In this study, we derived a novel peptide sequence and determined its antibacterial potentials.<\/jats:p><\/jats:sec><jats:sec><jats:title>Method:<\/jats:title><jats:p>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, beta-galactosidase, and molecular computational studies were conducted.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results:<\/jats:title><jats:p>AGAAN inhibited P. aeruginosa, E. faecalis, and S. typhimurium at 20 \u00b5M concentration. E. coli and S. aureus were inhibited at 25 \u00b5M, and lastly, B. subtilis at 50 \u00b5M. 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%\u20137.31% 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.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion:<\/jats:title><jats:p>AGAAN exhibits potential antibacterial properties that could be used to combat bacterial resistance.<\/jats:p><\/jats:sec>","DOI":"10.2174\/1389201021666201020161428","type":"journal-article","created":{"date-parts":[[2020,10,21]],"date-time":"2020-10-21T07:30:41Z","timestamp":1603265441000},"page":"1216-1227","update-policy":"https:\/\/doi.org\/10.2174\/bsp_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Antibacterial Potential of a Novel Peptide from the Consensus Sequence of Dermaseptin Related Peptides Secreted by Agalychnis annae"],"prefix":"10.2174","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9691-4194","authenticated-orcid":true,"given":"Ya\u2019u Sabo","family":"Ajingi","sequence":"first","affiliation":[{"name":"Department of Microbiology, Faculty of Science, King Mongkut\u2019s University of Technology Thonburi (KMUTT), Bangkok,Thailand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3713-4024","authenticated-orcid":true,"given":"Auwal","family":"Muhammad","sequence":"additional","affiliation":[{"name":"Theoretical and Computational Physics Group, Department of Physics, King Mongkut\u2019s University of Technology, Thonburi, (KMUTT),Thailand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pongsak","family":"Khunrae","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Faculty of Science, King Mongkut\u2019s University of Technology Thonburi (KMUTT), Bangkok,Thailand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Triwit","family":"Rattanarojpong","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Faculty of Science, King Mongkut\u2019s University of Technology Thonburi (KMUTT), Bangkok,Thailand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kovit","family":"Pattanapanyasat","sequence":"additional","affiliation":[{"name":"Office for Research and Development, Department of Immunology, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok,Thailand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4468-8885","authenticated-orcid":true,"given":"Thana","family":"Sutthibutpong","sequence":"additional","affiliation":[{"name":"Theoretical and Computational Physics Group, Department of Physics, King Mongkut\u2019s University of Technology, Thonburi, (KMUTT),Thailand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8839-2568","authenticated-orcid":true,"given":"Nujarin","family":"Jongruja","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Faculty of Science, King Mongkut\u2019s University of Technology Thonburi (KMUTT), Bangkok,Thailand"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"965","reference":[{"key":"ref=1","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1016\/j.nmni.2015.02.007","volume":"6","author":"Roca I.","year":"2015","unstructured":"Roca I.; Akova M.; Baquero F.; Carlet J.; Cavaleri M.; Coenen S.; Cohen J.; Findlay D.; Gyssens I.; Heuer O.E.; Kahlmeter G.; Kruse H.; Laxminarayan R.; Li\u00e9bana E.; L\u00f3pez-Cerero L.; MacGowan A.; Martins M.; Rodr\u00edguez-Ba\u00f1o J.; Rolain J.M.; Segovia C.; Sigauque B.; Tacconelli E.; Wellington E.; Vila J.; The global threat of antimicrobial resistance: Science for intervention. 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