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Issue 88, 2015
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Pb2+ binding to lentil lectin and its influence on the protein aggregation

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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

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Supplementary files

Article information


Submitted
10 Apr 2015
Accepted
12 Aug 2015
First published
14 Aug 2015

RSC Adv., 2015,5, 72352-72360
Article type
Paper

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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