Tuning the Activity of a Short Arg-Trp Antimicrobial Peptide by Lipidation of a C- or N-Terminal Lysine Side-Chain

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• 作者：H. Bauke Albada ; Pascal Prochnow ; Sandra Bobersky ; Sina Langklotz ; Patrick Schriek ; Julia E. Bandow ; Nils Metzler-Nolte
• 刊名：ACS Medicinal Chemistry Letters
• 出版年：2012
• 出版时间：December 13, 2012
• 年：2012
• 卷：3
• 期：12
• 页码：980-984
• 全文大小：234K
• 年卷期：v.3,no.12(December 13, 2012)
• ISSN：1948-5875

文摘

The attachment of lipids to C- or N-terminally positioned lysine side-chain amino groups increases the activity of a short synthetic (Arg-Trp)₃ antimicrobial peptide significantly, making these peptides even active against pathogenic Gram-negative bacteria. Thus, a peptide with strong activity against S. aureus (1.1鈥? 渭M) and good activity against A. baumannii and P. aeruginosa (9鈥?8 渭M) was identified. The most promising peptide causes 50% hemolysis at 285 渭M and shows some selectivity against human cancer cell lines. Interestingly, the increased activity of ferrocenoylated peptides is mostly due to the lipophilicity of the organometallic fragment.
<h4>Keywords: h4> hors" href="http://pubs.acs.org/action/doSearch?action=search&searchText=Lipidated+antimicrobial+peptides&qsSearchArea=searchText">Lipidated antimicrobial peptides; hors" href="http://pubs.acs.org/action/doSearch?action=search&searchText=ferrocenoyl&qsSearchArea=searchText">ferrocenoyl; hors" href="http://pubs.acs.org/action/doSearch?action=search&searchText=anticancer&qsSearchArea=searchText">anticancer; hors" href="http://pubs.acs.org/action/doSearch?action=search&searchText=nonhemolytic&qsSearchArea=searchText">nonhemolytic