5d2a
From Proteopedia
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==Bifunctional dendrimers== | ==Bifunctional dendrimers== | ||
<StructureSection load='5d2a' size='340' side='right' caption='[[5d2a]], [[Resolution|resolution]] 2.13Å' scene=''> | <StructureSection load='5d2a' size='340' side='right' caption='[[5d2a]], [[Resolution|resolution]] 2.13Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[5d2a]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D2A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5d2a]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D2A FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene>, <scene name='pdbligand=ZDC:3,7-ANHYDRO-2,8-DIDEOXY-L-GLYCERO-D-GLUCO-OCTONIC+ACID'>ZDC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene>, <scene name='pdbligand=ZDC:3,7-ANHYDRO-2,8-DIDEOXY-L-GLYCERO-D-GLUCO-OCTONIC+ACID'>ZDC</scene></td></tr> | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2a OCA], [http://pdbe.org/5d2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d2a RCSB], [http://www.ebi.ac.uk/pdbsum/5d2a PDBsum]</span></td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lecB, ERS445055_01627, PA8380_17510, PAE221_03716, PAMH19_1713, YQ19_10010 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> |
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2a OCA], [http://pdbe.org/5d2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d2a RCSB], [http://www.ebi.ac.uk/pdbsum/5d2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d2a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Antibiotic resistance in the opportunistic pathogen Pseudomonas aeruginosa is partly caused by biofilms forming a physical barrier to antibiotic penetration. Here we focused on modifying tetravalent glycopeptide dendrimer ligands of P. aeruginosa lectins LecB or LecA to increase their biofilm inhibition activity. First heteroglycoclusters were investigated displaying one pair each of LecB specific fucosyl groups and LecA specific galactosyl groups and binding simultaneously to both lectins, one of which gave the first fully resolved crystal structure of a peptide dendrimer as LecB complex providing a structural model for dendrimer-lectin interactions (PDB ; 5D2A). Biofilm inhibition was increased by introducing additional cationic residues in these dendrimers but resulted in bactericidal effects similar to those of non-glycosylated polycationic antimicrobial peptide dendrimers. In a second approach dendrimers displaying four copies of the natural LecB ligand Lewis(a) were prepared leading to slightly stronger LecB binding and biofilm inhibition. Finally synergistic application of a LecB specific non-bactericidal antibiofilm dendrimer with the antibiotic tobramycin at sub-inhibitory concentrations of both compounds allowed effective biofilm inhibition and dispersal. | ||
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+ | Overcoming antibiotic resistance in Pseudomonas aeruginosa biofilms using glycopeptide dendrimers.,Michaud G, Visini R, Bergmann M, Salerno G, Bosco R, Gillon E, Richichi B, Nativi C, Imberty A, Stocker A, Darbre T, Reymond JL Chem Sci. 2016 Jan 1;7(1):166-182. doi: 10.1039/c5sc03635f. Epub 2015 Nov 25. PMID:29896342<ref>PMID:29896342</ref> | ||
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+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5d2a" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 06:01, 11 July 2018
Bifunctional dendrimers
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Categories: Darbre, T | Michaud, G | Reymond, J L | Stocker, A | Visini, R | Bifunctional | Biofilm | Dendrimer | Lectinb | Pseudomona | Sugar binding protein