2nzz: Difference between revisions

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-[[Image:2nzz.jpg|left|200px]]<br /><applet load="2nzz" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2nzz" />
-'''NMR structure analysis of the Penetratin conjugated Gas (374-394) peptide'''<br />
-==Overview==
+==NMR structure analysis of the Penetratin conjugated Gas (374-394) peptide==
-A42 is a chimera peptide consisting of Galphas(374-394)C379A--the 21-mer C, terminus of the Galphas protein, able of adenosine inhibitory, activity--and penetratin--the 16 residue fragment, derived from the, homeodomain of the Drosophila transcription factor Antennapedia. A42 is, able to cross cell membranes and to inhibit A2A and A2B adenosine and, beta-adrenergic receptor stimulated camps (D'Ursi et al. Mol. Pharmacol., 2006, 69, 727-36). Here we present an extensive biophysical study of A42, in different membrane mimetics, with the objective to evaluate the, molecular mechanisms which promote the membrane permeation. Fluorescence, CD, and NMR data were acquired in the presence of negatively charged and, zwitterionic sodium dodecyl sulfate and dodecylphosphocholine surfactants., To validate the spectroscopic results in a larger scale, fluorescence, microscopy experiments were performed on negatively charged and, zwitterionic dipalmitoylphosphatidylglycerol and, dipalmitoylphosphatidylcholine vesicles. Our results show that the, internalization of A42 is mainly driven by electrostatic interactions, hydrophobic interactions playing only a secondary, sinergistic role. The, distribution of the charges along the molecule has an important role, highlighting that internalization is a process which requires a specific, matching of peptide and membrane properties.
+<StructureSection load='2nzz' size='340' side='right'caption='[[2nzz]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2nzz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NZZ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2nzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nzz OCA], [https://pdbe.org/2nzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nzz RCSB], [https://www.ebi.ac.uk/pdbsum/2nzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nzz ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A42 is a chimera peptide consisting of Galphas(374-394)C379A--the 21-mer C terminus of the Galphas protein, able of adenosine inhibitory activity--and penetratin--the 16 residue fragment, derived from the homeodomain of the Drosophila transcription factor Antennapedia. A42 is able to cross cell membranes and to inhibit A2A and A2B adenosine and beta-adrenergic receptor stimulated camps (D'Ursi et al. Mol. Pharmacol. 2006, 69, 727-36). Here we present an extensive biophysical study of A42 in different membrane mimetics, with the objective to evaluate the molecular mechanisms which promote the membrane permeation. Fluorescence, CD, and NMR data were acquired in the presence of negatively charged and zwitterionic sodium dodecyl sulfate and dodecylphosphocholine surfactants. To validate the spectroscopic results in a larger scale, fluorescence microscopy experiments were performed on negatively charged and zwitterionic dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine vesicles. Our results show that the internalization of A42 is mainly driven by electrostatic interactions, hydrophobic interactions playing only a secondary, sinergistic role. The distribution of the charges along the molecule has an important role, highlighting that internalization is a process which requires a specific matching of peptide and membrane properties.
-==About this Structure==
+Driving forces in the delivery of penetratin conjugated G protein fragment.,Albrizio S, Giusti L, D'Errico G, Esposito C, Porchia F, Caliendo G, Novellino E, Mazzoni MR, Rovero P, D'Ursi AM J Med Chem. 2007 Apr 5;50(7):1458-64. Epub 2007 Mar 10. PMID:17348636<ref>PMID:17348636</ref>
-NZZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZZ OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Driving forces in the delivery of penetratin conjugated G protein fragment., Albrizio S, Giusti L, D'Errico G, Esposito C, Porchia F, Caliendo G, Novellino E, Mazzoni MR, Rovero P, D'Ursi AM, J Med Chem. 2007 Apr 5;50(7):1458-64. Epub 2007 Mar 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17348636 17348636]
+</div>
-[[Category: Protein complex]]
+<div class="pdbe-citations 2nzz" style="background-color:#fffaf0;"></div>
-[[Category: Albrizio, S.]]
+== References ==
-[[Category: Errico, G.D.]]
+<references/>
-[[Category: Espsito, C.]]
+__TOC__
-[[Category: Novellino, E.]]
+</StructureSection>
-[[Category: Rovero, P.]]
+[[Category: Large Structures]]
-[[Category: Ursi, A.M.D.]]
+[[Category: Albrizio S]]
-[[Category: a2a adenosine receptor]]
+[[Category: D'Errico G]]
-[[Category: cell-penetrating peptides]]
+[[Category: D'Ursi AM]]
-[[Category: conformational analysis]]
+[[Category: Espsito C]]
-[[Category: g protein]]
+[[Category: Novellino E]]
-[[Category: gas subunit]]
+[[Category: Rovero P]]
-[[Category: nmr]]
-[[Category: penetratin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:01:00 2008''