{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T17:30:51Z","timestamp":1791307851798,"version":"4.3.1"},"reference-count":43,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2014,4,25]],"date-time":"2014-04-25T00:00:00Z","timestamp":1398384000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceuticals"],"abstract":"<jats:p>There is great interest in the development of antimicrobial peptides as a potentially novel class of antimicrobial agents. Several structural determinants are responsible for the antimicrobial and cytolytic activity of antimicrobial peptides. In our study,  a new synthetic peptide analog, AamAP1-Lysine from the naturally occurring scorpion venom antimicrobial peptide AamAP1, was designed by modifying the parent peptide in order to increase the positive charge and optimize other physico-chemical parameters involved in antimicrobial activity. AamAP1-Lysine displayed potent antibacterial activity against Gram-positive and Gram-negative bacteria. The minimum inhibitory concentration was in the range of 5 to 15 \u00b5M with a 10 fold increase in potency over the parent peptide. The hemolytic and antiproliferative activity of AamAP1-Lysine against eukaryotic mammalian cells was minimal at the concentration range needed to inhibit bacterial growth.  The antibacterial mechanism analysis indicated that AamAP1-Lysine is probably inducing bacterial cell death through membrane damage and permeabilization determined by the release of \u03b2-galactosidase enzyme from peptide treated E. coli cells. DNA binding studies revealed that AamAP1-Lysine caused complete retardation of DNA migration and could display intracellular activities in addition to the membrane permeabilization mode of action reported earlier. In conclusion, AamAP1-Lysine could prove to be a potential candidate for antimicrobial drug development in future studies.<\/jats:p>","DOI":"10.3390\/ph7050502","type":"journal-article","created":{"date-parts":[[2014,4,28]],"date-time":"2014-04-28T05:15:00Z","timestamp":1398662100000},"page":"502-516","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":44,"title":["Enhanced Antimicrobial Activity of AamAP1-Lysine,  a Novel Synthetic Peptide Analog Derived from  the Scorpion Venom Peptide AamAP1"],"prefix":"10.3390","volume":"7","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7804-3313","authenticated-orcid":false,"given":"Ammar","family":"Almaaytah","sequence":"first","affiliation":[{"name":"Department of Pharmaceutical Technology, Faculty of Pharmacy, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shadi","family":"Tarazi","sequence":"additional","affiliation":[{"name":"Department of Applied Biological Sciences, Faculty of Science and Arts,  Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahmad","family":"Abu-Alhaijaa","sequence":"additional","affiliation":[{"name":"Department of Applied Biological Sciences, Faculty of Science and Arts,  Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yara","family":"Altall","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Technology, Faculty of Pharmacy, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nizar","family":"Alshar'i","sequence":"additional","affiliation":[{"name":"Department of Medicinal Chemistry, Faculty of Pharmacy,  Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Khaldon","family":"Bodoor","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Genetic Engineering, Faculty of Science and Arts,  Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8350-900X","authenticated-orcid":false,"given":"Qosay","family":"Al-Balas","sequence":"additional","affiliation":[{"name":"Department of Medicinal Chemistry, Faculty of Pharmacy,  Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2014,4,25]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/j.arcmed.2005.06.009","article-title":"Resistance to antibiotics: Are we in the post-antibiotic era?","volume":"36","author":"Alanis","year":"2005","journal-title":"Arch. Med. Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/j.cell.2006.02.009","article-title":"Resistance to anti-infective drugs and the threat to public health","volume":"124","author":"Heymann","year":"2006","journal-title":"Cell"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"S25","DOI":"10.1016\/j.ijantimicag.2013.04.007","article-title":"Antimicrobial resistance: action to combat the rising microbial challenges","volume":"42","author":"Paphitou","year":"2013","journal-title":"Int. J. Antimicrob. 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