Alanine scanning studies of the antimicrobial peptide aurein 1.2
Dorian Migoń , Maciej Jaśkiewicz , Damian Neubauer , Marta Bauer , Emilia Sikorska , Elżbieta Kamysz , Wojciech Kamysz
AbstractAntimicrobial 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 helicitywas calculated from circular dichroismspectra. 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 series||Probiotics and Antimicrobial Proteins, ISSN 1867-1306, (A 20 pkt)|
|Publication size in sheets||0.6|
|Keywords in English||Aurein 1.2, antimicrobial peptides, structure-activity relationship, antimicrobial agents, peptide drugs, antibiotics|
|ASJC Classification||; ;|
|License||Other; published final; ; with publication|
|Score|| = 20.0, 03-04-2019, ArticleFromJournal|
= 20.0, 03-04-2019, ArticleFromJournal
|Publication indicators||: 2016 = 0.564; : 2017 = 2.345 (2) - 2017=2.091 (5)|
* presented citation count is obtained through Internet information analysis and it is close to the number calculated by the Publish or Perish system.