کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1392127 | 983707 | 2008 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Structure-Activity Relationships of Antibacterial Acyl-Lysine Oligomers Structure-Activity Relationships of Antibacterial Acyl-Lysine Oligomers](/preview/png/1392127.png)
SummaryWe describe structure-activity relationships that emerged from biophysical data obtained with a library of antimicrobial peptide mimetics composed of 103 oligoacyllysines (OAKs) designed to pin down the importance of hydrophobicity (H) and charge (Q). Based on results obtained with OAKs displaying minimal inhibitory concentration ≤ 3 μM, the data indicate that potent inhibitory activity of the gram-negative Escherichia coli and the gram-positive Staphylococcus aureus required a relatively narrow yet distinct window of HQ values where the acyl length played multiple and critical roles, both in molecular organization and in selective activity. Thus, incorporation of long—but not short—acyl chains within a peptide backbone is shown to lead to rigid supramolecular organization responsible for poor antibacterial activity and enhanced hemolytic activity. However, sequence manipulations, including introduction of a tandem lysine motif into the oligomer backbone, enabled disassembly of aggregated OAKs and subsequently revealed tiny, nonhemolytic, yet potent antibacterial derivatives.
Journal: - Volume 15, Issue 4, 21 April 2008, Pages 354–362