View source for 2mwl


==NMR structure of VG16KRKP, an antimicrobial peptide in LPS==
<StructureSection load='2mwl' size='340' side='right'caption='[[2mwl]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mwl]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MWL 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=2mwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwl OCA], [https://pdbe.org/2mwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mwl RCSB], [https://www.ebi.ac.uk/pdbsum/2mwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mwl ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The recent increase in multidrug resistance against bacterial infections has become a major concern to human health and global food security. Synthetic antimicrobial peptides (AMPs) have recently received substantial attention as potential alternatives to conventional antibiotics because of their potent broad-spectrum antimicrobial activity. These peptides have also been implicated in plant disease control for replacing conventional treatment methods that are polluting and hazardous to the environment and to human health. Here, we report de novo design and antimicrobial studies of VG16, a 16-residue active fragment of Dengue virus fusion peptide. Our results reveal that VG16KRKP, a non-toxic and non-hemolytic analogue of VG16, shows significant antimicrobial activity against Gram-negative E. coli and plant pathogens X. oryzae and X. campestris, as well as against human fungal pathogens C. albicans and C. grubii. VG16KRKP is also capable of inhibiting bacterial disease progression in plants. The solution-NMR structure of VG16KRKP in lipopolysaccharide features a folded conformation with a centrally located turn-type structure stabilized by aromatic-aromatic packing interactions with extended N- and C-termini. The de novo design of VG16KRKP provides valuable insights into the development of more potent antibacterial and antiendotoxic peptides for the treatment of human and plant infections.

Antimicrobial Peptides: Insights into Membrane Permeabilization, Lipopolysaccharide Fragmentation and Application in Plant Disease Control.,Datta A, Ghosh A, Airoldi C, Sperandeo P, Mroue KH, Jimenez-Barbero J, Kundu P, Ramamoorthy A, Bhunia A Sci Rep. 2015 Jul 6;5:11951. doi: 10.1038/srep11951. PMID:26144972<ref>PMID:26144972</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: Bhunia A]]
[[Category: Datta A]]