Issue 88, 2015

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

Abstract

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 β sheet to α-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.

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

Supplementary files

Article information

Article type
Paper
Submitted
10 Apr 2015
Accepted
12 Aug 2015
First published
14 Aug 2015

RSC Adv., 2015,5, 72352-72360

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

A. G. Thawari, K. Tabbasum, V. K. Hinge and C. P. Rao, RSC Adv., 2015, 5, 72352 DOI: 10.1039/C5RA06427A

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