6o8t
From Proteopedia
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==Syn-safencin 96== | ==Syn-safencin 96== | ||
| - | <StructureSection load='6o8t' size='340' side='right'caption='[[6o8t]]' scene=''> | + | <StructureSection load='6o8t' size='340' side='right'caption='[[6o8t]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[6o8t]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O8T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6O8T FirstGlance]. <br> |
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6o8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o8t OCA], [http://pdbe.org/6o8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o8t RCSB], [http://www.ebi.ac.uk/pdbsum/6o8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o8t ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6o8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o8t OCA], [http://pdbe.org/6o8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o8t RCSB], [http://www.ebi.ac.uk/pdbsum/6o8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o8t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ribosomally produced antimicrobial peptides of bacteria (bacteriocins) represent an unexplored source of membrane-active antibiotics. We designed a library of linear peptides from a circular bacteriocin and show that pore-formation dynamics in bacterial membranes are tunable via selective amino acid substitution. We observed antibacterial interpeptide synergy indicating that fundamentally altering interactions with the membrane enables synergy. Our findings suggest an approach for engineering pore-formation through rational peptide design and increasing the utility of novel antimicrobial peptides by exploiting synergy. | ||
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| + | Synthetic Antimicrobial Peptide Tuning Permits Membrane Disruption and Interpeptide Synergy.,Fields FR, Manzo G, Hind CK, Janardhanan J, Foik IP, Carmo Silva PD, Balsara RD, Clifford M, Vu HM, Ross JN, Kalwajtys VR, Gonzalez AJ, Bui TT, Ploplis VA, Castellino FJ, Siryaporn A, Chang M, Sutton JM, Mason AJ, Lee S ACS Pharmacol Transl Sci. 2020 Feb 21;3(3):418-424. doi:, 10.1021/acsptsci.0c00001. eCollection 2020 Jun 12. PMID:32566907<ref>PMID:32566907</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6o8t" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Fields | + | [[Category: Fields, F R]] |
| - | [[Category: Lee | + | [[Category: Lee, S W]] |
| + | [[Category: Antimicrobial]] | ||
| + | [[Category: Antimicrobial protein]] | ||
| + | [[Category: Synthetic peptide]] | ||
Revision as of 11:22, 22 July 2020
Syn-safencin 96
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