Record Details

Pb2+ binding to lentil lectin and its influence on the protein aggregation

DSpace at IIT Bombay

View Archive Info
 
 
Field Value
 
Title Pb2+ binding to lentil lectin and its influence on the protein aggregation
 
Creator THAWARI, AG
TABBASUM, K
HINGE, VK
RAO, CP
 
Subject CIRCULAR-DICHROISM
COORDINATION
SPECTROSCOPY
ALPHA
SIMULATIONS
TRANSITIONS
GLUTATHIONE
EXPOSURE
FORMS
IONS
 
Description Binding of Pb2+ to lentil lectin (LL) was studied by spectroscopy, microscopy and thermodynamics and the species were modelled by molecular dynamics (MD). The effect of pH on Pb2+ binding was studied at pH = 5 in acetate buffer and pH = 7.2 in Tris buffer. Based on ITC, multiple binding sites were found for Pb2+ at pH = 7.2. No binding is noticed at pH = 5. The MD results showed the involvement of aspartate and glutamate with hemi-directed geometry for Pb2+. Pb2+ mediated beta sheet to alpha-helix transition was noticed at pH = 7.2. At physiological pH, morphological changes were observed in the reduction of size of the particles of LL (160 +/- 30 nm) to those in {LL + Pb2+} (45 +/- 10 nm) as derived based on AFM and TEM. In presence of Pb2+, the larger particles break down to smaller ones because of the coordination ability of Pb2+ towards carboxylate and imidazole moieties. At pH = 5, the TEM shows much higher aggregation than that observed at pH = 7.2 for the protein alone, leading to linear aggregated species which were further broken down by Pb2+ into smaller ones.
 
Publisher ROYAL SOC CHEMISTRY
 
Date 2016-01-15T07:20:38Z
2016-01-15T07:20:38Z
2015
 
Type Article
 
Identifier RSC ADVANCES, 5(88)72352-72360
2046-2069
http://dx.doi.org/10.1039/c5ra06427a
http://dspace.library.iitb.ac.in/jspui/handle/100/18035
 
Language en