Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5WYE

Structure of gold nano particle-tagged VG16KRKP in Salmonella typhi LPS

Summary for 5WYE
Entry DOI10.2210/pdb5wye/pdb
NMR InformationBMRB: 36044
DescriptorAu-VG16KRKP (1 entity in total)
Functional Keywordsantimicrobial peptide, gold nanoparticle tagged, turn and loop type structure, amphipathic structure, antimicrobial protein
Biological sourceDengue virus
Total number of polymer chains1
Total formula weight1765.16
Authors
Ilyas, H.,Bhunia, A. (deposition date: 2017-01-12, release date: 2017-11-15, Last modification date: 2024-05-15)
Primary citationChowdhury, R.,Ilyas, H.,Ghosh, A.,Ali, H.,Ghorai, A.,Midya, A.,Jana, N.R.,Das, S.,Bhunia, A.
Multivalent gold nanoparticle-peptide conjugates for targeting intracellular bacterial infections
Nanoscale, 9:14074-14093, 2017
Cited by
PubMed Abstract: Although nanoparticle-tagged antimicrobal peptides have gained considerable importance in recent years, their structure-function correlation has not yet been explored. Here, we have studied the mechanism of action of a designed antimicrobial peptide, VG16KRKP (VARGWKRKCPLFGKGG), delivered via gold nanoparticle tagging against Salmonella infection by combining biological experiments with high- and low-resolution spectroscopic techniques. In comparison with the free VG16KRKP peptide or gold nanoparticle alone, the conjugated variant, Au-VG16KRKP, is non-cytotoxic to eukaryotic cells, but exhibits strong bacteriolytic activity in culture. Au-VG16KRKP can penetrate host epithelial and macrophage cells as well as interact with intracellular S. Typhi LPS under both in vitro and in vivo conditions. Treatment of mice with Au-VG16KRKP post-infection with S. Typhi resulted in reduced intracellular bacterial recovery and highly enhanced protection against S. Typhi challenge. The three-dimensional high resolution structure of nanoparticle conjugated VG16KRKP depicted the generation of a well-separated amphipathic structure with slight aggregation, responsible for the increase of the local concentration of the peptide, thus leading to potent activity. This is the first report on the structural and functional characterization of a nanoparticle conjugated synthetic antimicrobial peptide that can kill intracellular pathogens and eventually protect against S. Typhi challenge in vivo.
PubMed: 28901372
DOI: 10.1039/c7nr04062h
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon