Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/xmlui/handle/100/17281
Title: Mercuration of apo-alpha-lactalbumin: binding of Hg2+ followed by protein-mediated nanoparticle formation
Authors: THAWARI, AG
HINGE, VK
TEMGIRE, M
RAO, CP
Issue Date: 2014
Publisher: ROYAL SOC CHEMISTRY
Citation: RSC ADVANCES, 4(96)53429-53436
Abstract: Nanoparticles and nanocrystals of mercury are formed when Hg2+ salt reacts with apo-alpha-lactalbumin (apoa-alpha-LA). Reduction followed by nanoparticle formation is further augmented by the protein, as it also acts as a coating agent. The initial interaction of Hg2+ with apo-alpha-LA was demonstrated by changes observed in absorption, emission, and CD spectroscopy, where the latter technique also detected structural changes in the protein. Such structural changes are expected when Hg2+ binds to the protein, and therefore, the binding was determined by isothermal titration calorimetry (ITC). The binding was further proven by MALDI, which showed mercurated species of protein with a Gaussian distribution exhibiting a weighted average of 6 and 9 Hg2+ ions bound to protein when apo-alpha-LA was treated with 10 and 100 equivalents, respectively. The molecular dynamics studies revealed the binding of Hg2+ ions followed by the structural changes that occurred in the protein. The reaction between Hg2+ and apo-alpha-LA yields noncrystalline nanoparticles at lower molar ratios of Hg2+ and crystalline ones at higher molar ratios. The existence of both of these nanoparticles was proven by extensive TEM studies, and the mercury nanocrystals were further studied using fluorescence microscopy. X-ray photoelectron spectroscopy demonstrated that the protein has the ability to convert Hg2+ to Hg-0, and the resultant Hg-0 cluster is known to be less harmful than Hg2+ to the organism. All of these studies support the use of apo-alpha-LA in the form of nanoparticles and nanocrystals to detoxify Hg2+.
URI: http://dx.doi.org/10.1039/c4ra07156e
http://dspace.library.iitb.ac.in/jspui/handle/100/17281
ISSN: 2046-2069
Appears in Collections:Article

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.