Peptides: Rational Design of Membrane‐Pore‐Forming Peptides (Small 40/2017)
In article number 1701316, by Gisbert Schneider and co‐workers, a novel peptide descriptor enables the rational design of peptides based on their topological hydrophobic distribution. Applying this descriptor, a computational method generates an innovative peptide inspired by a natural template. Thi...
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Veröffentlicht in: | Small (Weinheim an der Bergstrasse, Germany) Germany), 2017-10, Vol.13 (40), p.n/a |
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Hauptverfasser: | , , , , , , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | In article number 1701316, by Gisbert Schneider and co‐workers, a novel peptide descriptor enables the rational design of peptides based on their topological hydrophobic distribution. Applying this descriptor, a computational method generates an innovative peptide inspired by a natural template. This peptide is then trialed and optimized for its ability to disrupt bacterial cells by forming ordered, pore‐like structures in membranes in an entropy‐driven mechanism. |
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ISSN: | 1613-6810 1613-6829 |
DOI: | 10.1002/smll.201770213 |