6b35
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR ensemble of Tyrocidine A analogue AC3.28== | |
| + | <StructureSection load='6b35' size='340' side='right' caption='[[6b35]], [[NMR_Ensembles_of_Models | 8 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6b35]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B35 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene>, <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6b34|6b34]]</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=6b35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b35 OCA], [http://pdbe.org/6b35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b35 RCSB], [http://www.ebi.ac.uk/pdbsum/6b35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b35 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The d-Phe-Pro beta-turn of the cyclic beta-hairpin antimicrobial decapeptide tyrocidine A, (Tyrc A) was substituted with the d-Phe-2-aminobenzoic acid (2-Abz) motif in a synthetic analogue (1). The NMR structure of 1 demonstrated that compound 1 retained the beta-hairpin structure of Tyrc A with additional planarity, resulting in approximately 30-fold reduced hemolysis than Tyrc A. Although antibacterial activity was partially compromised, a single Gln to Lys substitution (2) restored activity equivalent to Tyrc A against S. aureus, enhanced activity against two Gram negative strains and maintained the reduced hemeloysis of 1. Analysis by transmission electron microscopy (TEM) suggested a membrane lytic mechanism of action for these peptides. Compound 2 also exhibits nanomolar antifungal activity in synergy with amphotericin B. The d-Phe-2-Abz turn may serve as a tool for the synthesis of structurally predictable beta-hairpin libraries. Unlike traditional beta-turn motifs such as d-Pro-Gly, both the 2-Abz and d-Phe rings may be further functionalized. | ||
| - | + | Tyrocidine A Analogues Bearing the Planar d-Phe-2-Abz Turn Motif: How Conformation Impacts Bioactivity.,Cameron AJ, Edwards PJB, Harjes E, Sarojini V J Med Chem. 2017 Nov 28. doi: 10.1021/acs.jmedchem.7b00953. PMID:29140694<ref>PMID:29140694</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 6b35" style="background-color:#fffaf0;"></div> | |
| - | [[Category: Cameron, A | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cameron, A J]] | ||
| + | [[Category: Ewdards, P J.B]] | ||
[[Category: Harjes, E]] | [[Category: Harjes, E]] | ||
| + | [[Category: Sarojini, V]] | ||
| + | [[Category: Antimicrobial protein]] | ||
| + | [[Category: Tyrocidine a antimicrobial peptide amp cyclic peptide 2-aminobenzoic acid 2-abz anthranilic acid]] | ||
Revision as of 07:24, 6 December 2017
NMR ensemble of Tyrocidine A analogue AC3.28
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