7os8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR SOLUTION STRUCTURE OF [Pro3,DLeu9]TL== | |
| + | <StructureSection load='7os8' size='340' side='right'caption='[[7os8]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OS8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=7os8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7os8 OCA], [https://pdbe.org/7os8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7os8 RCSB], [https://www.ebi.ac.uk/pdbsum/7os8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7os8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The pharmacodynamic and pharmacokinetic properties of bioactive peptides can be modulated by introducing conformational constraints such as intramolecular macrocyclizations, which can involve either the backbone and/or side chains. Herein, we aimed at increasing the alpha-helicity content of temporin L, an isoform of an intriguing class of linear antimicrobial peptides (AMPs), endowed with a wide antimicrobial spectrum, by the employment of diverse side-chain tethering strategies, including lactam, 1,4-substituted [1,2,3]-triazole, hydrocarbon, and disulfide linkers. Our approach resulted in a library of cyclic temporin L analogues that were biologically assessed for their antimicrobial, cytotoxic, and antibiofilm activities, leading to the development of the first-in-class cyclic peptide related to this AMP family. Our results allowed us to expand the knowledge regarding the relationship between the alpha-helical character of temporin derivatives and their biological activity, paving the way for the development of improved antibiotic cyclic AMP analogues. | ||
| - | + | First-in-Class Cyclic Temporin L Analogue: Design, Synthesis, and Antimicrobial Assessment.,Bellavita R, Casciaro B, Di Maro S, Brancaccio D, Carotenuto A, Falanga A, Cappiello F, Buommino E, Galdiero S, Novellino E, Grossmann TN, Mangoni ML, Merlino F, Grieco P J Med Chem. 2021 Jul 23. doi: 10.1021/acs.jmedchem.1c01033. PMID:34296619<ref>PMID:34296619</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7os8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brancaccio D]] | ||
| + | [[Category: Carotenuto A]] | ||
Current revision
NMR SOLUTION STRUCTURE OF [Pro3,DLeu9]TL
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