Details

Autor(en) / Beteiligte

• Zikou, Sofia
• Koukkou, Anna-Irini
• Mastora, Panorea
• Sakarellos-Daitsiotis, Maria
• Sakarellos, Constantinos
• Drainas, Constantin
• Panou-Pomonis, Eygenia

Titel

Design and synthesis of cationic Aib-containing antimicrobial peptides: conformational and biological studies

Ist Teil von

• Journal of peptide science, 2007-07, Vol.13 (7), p.481-486

Ort / Verlag

Chichester, UK: John Wiley & Sons, Ltd

Erscheinungsjahr

2007

Quelle

Wiley Blackwell Single Titles

Beschreibungen/Notizen

• Development of antimicrobial peptides has attracted considerable attention in recent years due to the excessive use of antibiotics, which has led to multiresistant bacteria. Cationic amphiphilic Aib‐containing peptide models Ac‐(Aib‐Arg‐Aib‐Leu)n‐NH2, n = 1–4, and sequential cationic polypeptides (Arg‐X‐Gly)n, X = Ala, Val, Leu, were prepared and studied for their antimicrobial and hemolytic activity, as well as for their proteolytic stability. Ac‐(Aib‐Arg‐Aib‐Leu)n‐NH2, n = 2, 3 and the polypeptide (Arg‐Leu‐Gly)n exhibited significant antimicrobial activity, and they were nontoxic at their MIC values and resistant, in particular the Aib‐peptide models, to enzymatic degradation. The conformational characteristics of the peptide models were studied by circular dichroism (CD). Structure‐activity relationship studies revealed the importance of the amphipathic α‐helical conformation of the reported peptides in inducing antimicrobial effects. It is concluded that peptide models comprising cationic amino acids (Arg), helicogenic and noncoding residues (Aib) and/or hydrophobic and helix‐promoting components (Leu) may lead to the development of antimicrobial therapeutics. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.