News Column

New Findings from Bhabha Atomic Research Center in the Area of Protein Nanoparticles Reported (Protein nanoparticle electrostatic interaction: Size...

July 8, 2014



New Findings from Bhabha Atomic Research Center in the Area of Protein Nanoparticles Reported (Protein nanoparticle electrostatic interaction: Size dependent counterions induced conformational change of hen egg white lysozyme)

By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Protein Nanoparticles have been published. According to news reporting from Maharashtra, India, by NewsRx journalists, research stated, "In our earlier paper (Ghosh et al., 2013), we have shown that (i) the positively charged hen egg white lysozyme (HEWL), dispersed in water, binds electrostatically with the negatively functionalized iron oxide nanoparticles (IONPs), and (ii) the Na+ counterions, associated with functionalized IONPs, diffuse into bound proteins and irreversibly unfold them. Having this information, we have extended our investigation and report here the effect of the size and the charge of alkaline metal counterions on the conformational modification of HEWL."

The news correspondents obtained a quote from the research from Bhabha Atomic Research Center, "In order to obtain a negative functional 'shell' on IONPs and the counterions of different size and charge we have functionalized IONPs with different derivatives of citrate, namely, tri-lithium citrate (TLC, Li3C6H5O7), tri-sodium citrate (TSC, Na3C6H5O7), tri-potassium citrate (TKC, K3C6H5O7) and tri-magnesium citrate (TMC, Mg3C12H10O14). The size of counterions varies as Mg2+ < Li+ < Na+ < K+. After interaction with the functionalized IONPs, the unfolding of HEWL was the maximum in presence of Li+ and was decreasing with increasing size of counterions. The UV-vis absorption measurements indicated that the unfolding of HEWL was due to modification in the hydrophobic environment around the tryptophan regions. The unfolding of HEWL was associated with the change of folding conformation from the alpha-helix to the beta-sheet. In absence of counterions, ligand-IONPs have no effect on the native conformation of HEWL."

According to the news reporters, the research concluded: "An effective use of counterions in order to modify protein conformation (and, the functionality) via protein-nanoparticle electrostatic interaction is a new finding, and be useful for an alternative medical therapy."

For more information on this research see: Protein nanoparticle electrostatic interaction: Size dependent counterions induced conformational change of hen egg white lysozyme. Colloids and Surfaces B-Biointerfaces, 2014;118():1-6. Colloids and Surfaces B-Biointerfaces can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands (see also Protein Nanoparticles).

Our news journalists report that additional information may be obtained by contacting G. Ghosh, Bhabha Atom Res Center, Div Chem, Bombay 400085, Maharashtra, India. Additional authors for this research include L. Panicker and K.C. Barick.

Keywords for this news article include: Asia, India, Lysozyme, Maharashtra, Nanotechnology, Emerging Technologies, Protein Nanoparticles

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


For more stories covering the world of technology, please see HispanicBusiness' Tech Channel



Source: Life Science Weekly


Story Tools






HispanicBusiness.com Facebook Linkedin Twitter RSS Feed Email Alerts & Newsletters