دورية أكاديمية
Enhanced Antimicrobial Activity of AamAP1-Lysine, a Novel Synthetic Peptide Analog Derived from the Scorpion Venom Peptide AamAP1
| العنوان: | Enhanced Antimicrobial Activity of AamAP1-Lysine, a Novel Synthetic Peptide Analog Derived from the Scorpion Venom Peptide AamAP1 |
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| المؤلفون: | Ammar Almaaytah, Shadi Tarazi, Ahmad Abu-Alhaijaa, Yara Altall, Nizar Alshar'i, Khaldon Bodoor, Qosay Al-Balas |
| المصدر: | Pharmaceuticals, Vol 7, Iss 5, Pp 502-516 (2014) |
| بيانات النشر: | MDPI AG, 2014. |
| سنة النشر: | 2014 |
| المجموعة: | LCC:Medicine LCC:Pharmacy and materia medica |
| مصطلحات موضوعية: | antimicrobial peptides, peptide design, membrane-permeation, scorpion peptide, molecular modeling, Medicine, Pharmacy and materia medica, RS1-441 |
| الوصف: | 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. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 1424-8247 |
| العلاقة: | http://www.mdpi.com/1424-8247/7/5/502Test; https://doaj.org/toc/1424-8247Test |
| DOI: | 10.3390/ph7050502 |
| الوصول الحر: | https://doaj.org/article/f68ed3cc83774dc2b85d20add0946454Test |
| رقم الانضمام: | edsdoj.f68ed3cc83774dc2b85d20add0946454 |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 14248247 |
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| DOI: | 10.3390/ph7050502 |