Antimicrobial Peptides Derived from Fusion Peptides of Influenza A Viruses, a Promising Approach to Designing Potent Antimicrobial Agents. (6th February 2015)

• Record Type: Journal Article
• Authors: Wang, Jingyu; Zhong, Wenjing; Lin, Dongguo; Xia, Fan; Wu, Wenjiao; Zhang, Heyuan; Lv, Lin; Liu, Shuwen; He, Jian
• Is Part Of: Chemical biology & drug design. Volume 86:Number 4(2015:Oct.)
• Page Start: 487
• Page End: 495
• Publication Date: 2015-02-06
• Subjects: Drugs -- Design -- Periodicals; Pharmaceutical chemistry -- Periodicals; Biochemistry -- Periodicals; 615.19005
• DOI: 10.1111/cbdd.12511
• Languages: English
• ISSNs: 1747-0277

Abstract

<abstract abstract-type="main" id="cbdd12511-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The emergence and dissemination of antibiotic‐resistant bacterial pathogens have spurred the urgent need to develop novel antimicrobial agents with different mode of action. In this respect, we turned several fusogenic peptides (FPs) derived from the hemagglutinin glycoproteins (HAs) of IAV into potent antibacterials by replacing the negatively or neutrally charged residues of FPs with positively charged lysines. Their antibacterial activities were evaluated by testing the MICs against a panel of bacterial strains including <italic>S. aureus, S. mutans, P</italic>. <italic>aeruginosa, </italic> and <italic>E. coli</italic>. The results showed that peptides HA‐FP‐1, HA‐FP‐2‐1, and HA‐FP‐3‐1 were effective against both Gram‐positive and Gram‐negative bacteria with MICs ranging from 1.9 to 16.0 <italic>μ</italic><sc>m</sc>, while the toxicities toward mammalian cells were low. In addition, the mode of action and the secondary structure of these peptides were also discussed. These data not only provide several potent peptides displaying promising potential in development as broad antimicrobial agents, but also present a useful strategy in designing new antimicrobial agents.</p> </abstract>