7osd
From Proteopedia
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<StructureSection load='7osd' size='340' side='right'caption='[[7osd]]' scene=''> | <StructureSection load='7osd' size='340' side='right'caption='[[7osd]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OSD FirstGlance]. <br> |
| - | </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=7osd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7osd OCA], [https://pdbe.org/7osd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7osd RCSB], [https://www.ebi.ac.uk/pdbsum/7osd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7osd ProSAT]</span></td></tr> | + | </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=7osd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7osd OCA], [https://pdbe.org/7osd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7osd RCSB], [https://www.ebi.ac.uk/pdbsum/7osd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7osd ProSAT]</span></td></tr> | ||
</table> | </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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7osd" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
NMR Solution Structure of Peptide 12: First-in-class cyclic Temporin L analogue with antibacterial and antibiofilm activities
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