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.
journal_name
Probiotics Antimicrob Proteinsjournal_title
Probiotics and antimicrobial proteinsauthors
Migoń D,Jaśkiewicz M,Neubauer D,Bauer M,Sikorska E,Kamysz E,Kamysz Wdoi
10.1007/s12602-018-9501-0subject
Has Abstractpub_date
2019-09-01 00:00:00pages
1042-1054issue
3eissn
1867-1306issn
1867-1314pii
10.1007/s12602-018-9501-0journal_volume
11pub_type
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