期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1828, 期 2, 页码 652-660出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2012.08.027
关键词
Antimicrobial peptide; Temporin L; D-Amino acid; Peptide-membrane interaction; Drug-resistance; NMR spectroscopy
资金
- Sapienza Universita di Roma
- Italian Ministero dell'Istruzione, Universita e Ricerca
- CNR, Istituto di Biologia e Patologia Molecolari
The frog skin peptide temporin L (TL, 13-residues long) has a wide and potent spectrum of antimicrobial activity, but it is also toxic on mammalian cells at its microbicidal concentrations. Previous studies have indicated that its analogue [Pro(3)]TL has a slightly reduced hemolytic activity and a stable helical conformation along residues 6-13. Here, to expand our knowledge on the relationship between the extent/position of alpha-helix in TL and its biological activities, we systematically replaced single amino acids within the alpha-helical domain of [Pro(3)]TL with the corresponding D isomers, known as helix breakers. Structure-activity relationship studies of these analogues, by means of CD and NMR spectroscopy analyses as well as antimicrobial and hemolytic assays were performed. Besides increasing our understanding on the structural elements that are responsible for cell selectivity of TL, this study revealed that a single L to D amino acid substitution can preserve strong anti-Candida activity of [Pro(3)]TL, without giving a toxic effect towards human cells. (C) 2012 Elsevier B.V. All rights reserved.
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