2n8d
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n8d OCA], [http://pdbe.org/2n8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n8d RCSB], [http://www.ebi.ac.uk/pdbsum/2n8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n8d ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n8d OCA], [http://pdbe.org/2n8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n8d RCSB], [http://www.ebi.ac.uk/pdbsum/2n8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n8d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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-pore-forming 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-in-class 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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| + | Rational Design of Membrane-Pore-Forming Peptides.,Pillong M, Hiss JA, Schneider P, Lin YC, Posselt G, Pfeiffer B, Blatter M, Muller AT, Bachler S, Neuhaus CS, Dittrich PS, Altmann KH, Wessler S, Schneider G Small. 2017 Aug 11. doi: 10.1002/smll.201701316. PMID:28799716<ref>PMID:28799716</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2n8d" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 04:17, 30 August 2017
In silico designed antimicrobial peptide Lavracin
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