期刊
SMALL
卷 13, 期 40, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/smll.201701316
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资金
- Swiss National Science Foundation [205321-134783, 206021-133768, 200021-157190, CRSII2_160699]
- Swiss National Science Foundation (SNF) [CRSII2_160699, 206021_133768] Funding Source: Swiss National Science Foundation (SNF)
Specific interactions of peptides with lipid membranes are essential for cellular communication and constitute a central aspect of the innate host defense against pathogens. A computational method for generating innovative membrane-poreforming peptides inspired by natural templates is presented. Peptide representation in terms of sequence-and topology-dependent hydrophobic moments is introduced. This design concept proves to be appropriate for the de novo generation of first-inclass membrane-active peptides with the anticipated mode of action. The designed peptides outperform the natural template in terms of their antibacterial activity. They form a kinked helical structure and self-assemble in the membrane by an entropy-driven mechanism to form dynamically growing pores that are dependent on the lipid composition. The results of this study demonstrate the unique potential of natural template-based peptide design for chemical biology and medicinal chemistry.
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