Abstract
Antimicrobial peptides (AMPs) are compounds widely distributed in nature that display activity against a broad spectrum of pathogens. Amphibian skin, as an organ rich in pharmacologically active peptides, appears to be an interesting source of novel AMPs. Aurein 1.2 (GLFDIIKKIAESF-NH2) is a short 13-residue antimicrobial peptide primarily isolated from the skin secretions of Australian bell frogs. In this study, the alanine scan of aurein 1.2 was performed to investigate the effect of each amino acid residue on its biological and physico-chemical properties. The biological studies included determination of minimum inhibitory concentration, activity against biofilm, and inhibitory effect on its formation. Moreover, the hemolytic activity as well as serum stability was determined. The hydrophobicity of peptides and their self-assembly were investigated using reversed-phase chromatography. In addition, their helicity was calculated from circular dichroism spectra. The results not only provided information on structure-activity relationship of aurein 1.2 but also gave insights into design of novel analogs of AMPs in the future.
Highlights
An increasing resistance to antibiotics among microorganisms looms a serious threat to human society
The highest activity was found against S. aureus with Minimum biofilm eradication concentrations (MBECs) value of 16 μg/mL, which was 4-fold lower than that of aurein 1.2
It is noteworthy that analog S12A was as active as parent molecule against C. albicans biofilm, while other analogs exhibited higher MBEC
Summary
An increasing resistance to antibiotics among microorganisms looms a serious threat to human society. According to the Review on Antimicrobial Resistance, at least 700,000 annual deaths are caused by drug-resistant infections This number was estimated to soar up to 10 million in 2050, if only the current antibiotic politics remain unchanged [1]. Aurein 1.2 (GLFDIIKKIAESF-NH2) is a short 13residue antimicrobial peptide with molecular mass of approximately 1480 Da and positive (+ 1) net charge at physiological pH. It was initially isolated from Australian bell frogs, Ranoidea aurea (formerly Litoria aurea) and Ranoidea raniformis (formerly L. raniformis) skin secretions [10]. Anticancer activity of aurein 1.2 has been demonstrated through the NCI-60 human tumor cell lines [14]. Laadhari et al in their in vivo studies suggest that antimicrobial activity of aurein 1.2 is an effect of membrane destabilization and/or disruption, and interactions between the peptide and bacterial teichoic acid and lipoteichoic acid should be considered [17]
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