Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa
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 characteri...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-11-01
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| Series: | Heliyon |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405844022026330 |
| _version_ | 1811213533350723584 |
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| author | Minakshi Maity Ushasi Pramanik Venkatesha R. Hathwar Paula Brandao Saptarshi Mukherjee Swapan Maity Ribhu Maity Tithi Maity Bidhan Chandra Samanta |
| author_facet | Minakshi Maity Ushasi Pramanik Venkatesha R. Hathwar Paula Brandao Saptarshi Mukherjee Swapan Maity Ribhu Maity Tithi Maity Bidhan Chandra Samanta |
| author_sort | Minakshi Maity |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T05:48:07Z |
| format | Article |
| id | doaj.art-186e9f5e1ac4451b961f7361916f0043 |
| institution | Directory Open Access Journal |
| issn | 2405-8440 |
| language | English |
| last_indexed | 2024-04-12T05:48:07Z |
| publishDate | 2022-11-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Heliyon |
| spelling | doaj.art-186e9f5e1ac4451b961f7361916f00432022-12-22T03:45:23ZengElsevierHeliyon2405-84402022-11-01811e11345Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHaMinakshi Maity0Ushasi Pramanik1Venkatesha R. Hathwar2Paula Brandao3Saptarshi Mukherjee4Swapan Maity5Ribhu Maity6Tithi Maity7Bidhan Chandra Samanta8Department of Chemistry, Mugberia Gangadhar Mahavidyalaya, Bhupatinagar, Purba Medinipur, 721425, West Bengal, IndiaDepartment of Chemistry, IISER Bhopal, Bhopal Bypass Road, Bhauri, Bhopal 462 066, Madhya Pradesh, IndiaSchool of Physical and Applied Sciences, Goa University, Taleigao Plateau, Goa 403 206, IndiaDepartamento de Química/CICECO, Universidade de Aveiro, 3810-193 Aveiro, PortugalDepartment of Chemistry, IISER Bhopal, Bhopal Bypass Road, Bhauri, Bhopal 462 066, Madhya Pradesh, IndiaSchool of Materials Science and Technology (SMST), Indian Institute of Technology (IIT), BHU, IndiaDepartment of Chemistry, Mugberia Gangadhar Mahavidyalaya, Bhupatinagar, Purba Medinipur, 721425, West Bengal, IndiaDepartment of Chemistry, Prabhat Kumar College, Purba Medinipur, Contai, 721401, West Bengal, IndiaDepartment of Chemistry, Mugberia Gangadhar Mahavidyalaya, Bhupatinagar, Purba Medinipur, 721425, West Bengal, India; Corresponding author.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.http://www.sciencedirect.com/science/article/pii/S2405844022026330BSA quencherCu(II) complexCytotoxicitySchiff baseSiHa cancer cell |
| spellingShingle | Minakshi Maity Ushasi Pramanik Venkatesha R. Hathwar Paula Brandao Saptarshi Mukherjee Swapan Maity Ribhu Maity Tithi Maity Bidhan Chandra Samanta Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa Heliyon BSA quencher Cu(II) complex Cytotoxicity Schiff base SiHa cancer cell |
| title | Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa |
| title_full | Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa |
| title_fullStr | Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa |
| title_full_unstemmed | Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa |
| title_short | Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa |
| title_sort | biophysical insights into the binding capability of cu ii schiff base complex with bsa protein and cytotoxicity studies against siha |
| topic | BSA quencher Cu(II) complex Cytotoxicity Schiff base SiHa cancer cell |
| url | http://www.sciencedirect.com/science/article/pii/S2405844022026330 |
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