Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa

Detalhes bibliográficos
Autor(a) principal: Maity, Minakshi
Data de Publicação: 2022
Outros Autores: Pramanik, Ushasi, Hathwar, Venkatesha R., Brandão, Paula, Mukherjee, Saptarshi, Maity, Swapan, Maity, Ribhu, Maity, Tithi, Chandra Samanta, Bidhan
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10773/36476
Resumo: 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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spelling Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHaBSA quencherCu(II) complexCytotoxicitySchiff baseSiHaCancer cellHerein, 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.Elsevier2023-03-06T15:26:18Z2022-11-01T00:00:00Z2022-11info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/36476eng10.1016/j.heliyon.2022.e11345Maity, MinakshiPramanik, UshasiHathwar, Venkatesha R.Brandão, PaulaMukherjee, SaptarshiMaity, SwapanMaity, RibhuMaity, TithiChandra Samanta, Bidhaninfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-02-22T12:09:50Zoai:ria.ua.pt:10773/36476Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:07:05.364047Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa
title Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa
spellingShingle Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa
Maity, Minakshi
BSA quencher
Cu(II) complex
Cytotoxicity
Schiff base
SiHa
Cancer cell
title_short 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_sort Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa
author Maity, Minakshi
author_facet Maity, Minakshi
Pramanik, Ushasi
Hathwar, Venkatesha R.
Brandão, Paula
Mukherjee, Saptarshi
Maity, Swapan
Maity, Ribhu
Maity, Tithi
Chandra Samanta, Bidhan
author_role author
author2 Pramanik, Ushasi
Hathwar, Venkatesha R.
Brandão, Paula
Mukherjee, Saptarshi
Maity, Swapan
Maity, Ribhu
Maity, Tithi
Chandra Samanta, Bidhan
author2_role author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Maity, Minakshi
Pramanik, Ushasi
Hathwar, Venkatesha R.
Brandão, Paula
Mukherjee, Saptarshi
Maity, Swapan
Maity, Ribhu
Maity, Tithi
Chandra Samanta, Bidhan
dc.subject.por.fl_str_mv BSA quencher
Cu(II) complex
Cytotoxicity
Schiff base
SiHa
Cancer cell
topic BSA quencher
Cu(II) complex
Cytotoxicity
Schiff base
SiHa
Cancer cell
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.
publishDate 2022
dc.date.none.fl_str_mv 2022-11-01T00:00:00Z
2022-11
2023-03-06T15:26:18Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10773/36476
url http://hdl.handle.net/10773/36476
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1016/j.heliyon.2022.e11345
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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