6qxc
From Proteopedia
(Difference between revisions)
m (Protected "6qxc" [edit=sysop:move=sysop]) |
|||
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==NMR structure of peptide 8, characterized by a trans-4-cyclohexyl-Pro, with a dramatic reduction in activity on E. coli ATCC and lost effect on P. aeruginosa.== | |
| + | <StructureSection load='6qxc' size='340' side='right'caption='[[6qxc]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6qxc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudis_bolbodactyla Pseudis bolbodactyla]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QXC FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PH6:(4S)-4-CYCLOHEXYL-L-PROLINE'>PH6</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qxc OCA], [https://pdbe.org/6qxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qxc RCSB], [https://www.ebi.ac.uk/pdbsum/6qxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qxc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Previously, we identified a potent antimicrobial analogue of temporin L (TL), [Pro3]TL, in which glutamine at position 3 was substituted with proline. In this study, a series of analogues, where the position 3 was substituted with non-natural proline derivatives, was investigated for the correlation between the conformational properties of the compounds and their antibacterial, cytotoxic and hemolytic activities. Non-natural proline analogues with substituents at position 4 of the pyrrolidine ring were considered. Structure-activity relationship studies of these analogues were performed by means of antimicrobial and cytotoxicity assays along with circular dichroism (CD) and NMR spectroscopy analysis for selected compounds. The most promising peptides were additionally evaluated for their activity against some representative veterinary microbial strains to compare with those from human strains. We identified novel analogues with interesting properties that make them attractive lead compounds. | ||
| - | + | The Outcomes of Decorated-Prolines in Discovering Novel Antimicrobial Peptides from Temporin-L.,Grieco P, Buommino E, Carotenuto A, Antignano I, Bellavita R, Casciaro B, Loffredo MR, Merlino F, Novellino E, Mangoni ML, Nocera FP, Brancaccio D, Punzi P, Roversi D, Ingenito R, Bianchi E ChemMedChem. 2019 May 14. doi: 10.1002/cmdc.201900221. PMID:31087626<ref>PMID:31087626</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6qxc" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Merlino | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudis bolbodactyla]] | ||
| + | [[Category: Brancaccio D]] | ||
| + | [[Category: Carotenuto A]] | ||
| + | [[Category: Grieco P]] | ||
| + | [[Category: Merlino F]] | ||
| + | [[Category: Novellino E]] | ||
Current revision
NMR structure of peptide 8, characterized by a trans-4-cyclohexyl-Pro, with a dramatic reduction in activity on E. coli ATCC and lost effect on P. aeruginosa.
| |||||||||||
