View source for 5ykk


==Antimicrobial peptide Andersonin-Y1 (AY1)==
<StructureSection load='5ykk' size='340' side='right'caption='[[5ykk]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ykk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Odorrana_andersonii Odorrana andersonii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YKK 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=5ykk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ykk OCA], [https://pdbe.org/5ykk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ykk RCSB], [https://www.ebi.ac.uk/pdbsum/5ykk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ykk ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The recent rise of multidrug resistant microbial strains requires development of new and novel therapeutic alternatives. In this study, we present a novel antibacterial system that comprises of modified naturally abundant antimicrobial peptides in conjugation with silver nanoparticles. Further, we propose a simple route to incorporate a cysteine residue either at the N- or C-terminal of the parent peptide. Tagging a cysteine residue at the terminals not only enhances the binding propensity of the resultant peptide with the silver nanoparticle, but also increases its antimicrobial property against several pathogenic bacterial strains including K. pneumoniae. The minimum inhibitory concentration (MIC) values of the cysteine tagged nanoconjugates were obtained in the range of 5-15 muM compared to 50 muM for peptides devoid of the cysteines. The origin and mechanism of such improved activity of the conjugates were investigated using NMR spectroscopy and molecular dynamics (MD) simulations. The application of (13)C-isotope labelled media to track the metabolic lifecycle of E. coli cells provided further insights into the system. MD simulations showed that pore formation in membrane bilayer is mediated through a hydrophobic collapse mechanism. The design strategy described herein opens up new-avenues for using biocompatible nanomedicines as a potential alternative to conventional antibiotics.

A Peptide-Nanoparticle System with Improved Efficacy against Multidrug Resistant Bacteria.,Pal I, Bhattacharyya D, Kar RK, Zarena D, Bhunia A, Atreya HS Sci Rep. 2019 Mar 14;9(1):4485. doi: 10.1038/s41598-019-41005-7. PMID:30872680<ref>PMID:30872680</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Odorrana andersonii]]
[[Category: Atreya HS]]
[[Category: Bhunia A]]
[[Category: Pal I]]