7os8: Difference between revisions

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==NMR SOLUTION STRUCTURE OF [Pro3,DLeu9]TL==

== Structural highlights ==

<table><tr><td colspan='2'>Full ~~crystallographic~~ 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>

<table><tr><td colspan='2'>[[7os8]] is a 1 chain structure. 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='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>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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>

== 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>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Brancaccio D]]

[[Category: Brancaccio, D]]

[[Category: Carotenuto A]]

[[Category: Carotenuto, A]]

[[Category: Antimicrobial protein]]

[[Category: Antimicrobic]]

[[Category: Conformational analysis]]

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@@ Line 1: / Line 1: @@
 ==NMR SOLUTION STRUCTURE OF [Pro3,DLeu9]TL==
-<StructureSection load='7os8' size='340' side='right'caption='[[7os8]]' scene=''>
+<StructureSection load='7os8' size='340' side='right'caption='[[7os8]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic 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>
+<table><tr><td colspan='2'>[[7os8]] is a 1 chain structure. 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='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>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7os8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Brancaccio D]]
+[[Category: Brancaccio, D]]
-[[Category: Carotenuto A]]
+[[Category: Carotenuto, A]]
+[[Category: Antimicrobial protein]]
+[[Category: Antimicrobic]]
+[[Category: Conformational analysis]]