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Updated: Aug 21, 2025

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity
Minakshi Maity1, Ushasi Pramanik2, Venkatesha R Hathwar3
1Department of Chemistry, Mugberia Gangadhar Mahavidyalaya, Bhupatinagar, Purba Medinipur, 721425, West Bengal, India.
Abstract:
Herein, we have explored the effects of chlorinated mononuclear Cu(II) complex upon binding with BSA protein (bovine serum albumin) and its in vitro anti-proliferative potentiality against SiHa cell. The complex was synthesized involving a Schiff base ligand having N,N,O donor centers and characterized by several spectroscopic studies. Structure, DFT studies and Hirshfeld surface (HS) analyses were identified using crystallographic computational studies. The binding interaction with BSA depicts the efficacy of the complex towards promising binding of it with BSA. Further, the complex shows a moderate cytotoxicity against SiHa cancer cell signifying its potentiality as an anti-proliferative agent for human cervix uteri carcinoma.
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