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Pharmaceuticals 2014, 7(5), 502-516; doi:10.3390/ph7050502
Article

Enhanced Antimicrobial Activity of AamAP1-Lysine, a Novel Synthetic Peptide Analog Derived from the Scorpion Venom Peptide AamAP1

1,* , 2
, 2
, 1
, 3
, 4
 and 3
1 Department of Pharmaceutical Technology, Faculty of Pharmacy, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan 2 Department of Applied Biological Sciences, Faculty of Science and Arts, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan 3 Department of Medicinal Chemistry, Faculty of Pharmacy, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan 4 Department of Biotechnology and Genetic Engineering, Faculty of Science and Arts, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, Jordan
* Author to whom correspondence should be addressed.
Received: 7 March 2014 / Revised: 9 April 2014 / Accepted: 14 April 2014 / Published: 25 April 2014
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Abstract

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 µM 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 β-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.
Keywords: antimicrobial peptides; peptide design; membrane-permeation; scorpion peptide; molecular modeling antimicrobial peptides; peptide design; membrane-permeation; scorpion peptide; molecular modeling
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Almaaytah, A.; Tarazi, S.; Abu-Alhaijaa, A.; Altall, Y.; Alshar'i, N.; Bodoor, K.; Al-Balas, Q. Enhanced Antimicrobial Activity of AamAP1-Lysine, a Novel Synthetic Peptide Analog Derived from the Scorpion Venom Peptide AamAP1. Pharmaceuticals 2014, 7, 502-516.

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