Peptides: Rational Design of Membrane‐Pore‐Forming Peptides (Small 40/2017)
Source abstract
Abstract
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.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Antimicrobial Peptides and Activities · Chemical Synthesis and Analysis · Supramolecular Self-Assembly in Materials
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Affiliations
Department of Chemistry and Applied Biosciences ETH Zurich 8093 Zurich Switzerland
Department of Molecular Biology University of Salzburg 5020 Salzburg Austria
Department of Biosystems Science and Engineering ETH Zurich 8093 Zurich Switzerland
References
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