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Probing the binding effects of zinc and cadmium with garlic phytocystatin: Implication of the abiotic stress on garlic phytocystatin

Abiotic stress induced by heavy metals retards the growth and development of plants. Therefore, it is essential to have an insight into the potential toxic effects of heavy metals. The present article investigates the effect of zinc and cadmium on the structure and function of garlic phytocystatin (...

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Bibliographic Details
Published in:International journal of biological macromolecules 2019-07, Vol.133, p.945-956
Main Authors: Siddiqui, Mohd Faizan, Bano, Bilqees
Format: Article
Language:English
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Summary:Abiotic stress induced by heavy metals retards the growth and development of plants. Therefore, it is essential to have an insight into the potential toxic effects of heavy metals. The present article investigates the effect of zinc and cadmium on the structure and function of garlic phytocystatin (GPhyCys). The cysteine proteinase inhibitory assay showed a reduction in the inhibitory activity upon binding with zinc and cadmium. UV–vis absorption spectroscopy revealed the complex formation of zinc and cadmium with garlic phytocystatin. Fluorescence quenching experiment confirmed the quenching of fluorophores upon binding of zinc and cadmium. Synchronous and 3-dimensional fluorescence spectroscopy suggest the alteration in the microenvironment around aromatic residues of garlic phytocystatin upon binding with the above metals. Circular dichroism showed a reduction in the alpha-helical content of native garlic phytocystatin. Scanning electron micrographs showed the morphological changes in the native garlic phytocystatin upon addition of zinc and cadmium. The observations confirmed the alteration in structure and conformation of garlic phytocystatin upon interaction with zinc and cadmium. It can be safely concluded that the high concentration of zinc and cadmium can alter the functioning of cysteine proteinase present in garlic and affects the growth and development of plants. •Zinc and cadmium bind to garlic phytocystatin with high affinity.•Decrease in cysteine proteinase inhibitory activity of garlic phytocystatin upon interaction with zinc and cadmium.•Binding of zinc and cadmium disrupts the conformation in the micro-environment around aromatic residues.•Secondary structure of garlic phytocystatin gets altered upon binding of zinc and cadmium.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2019.04.036