In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes

Detalhes bibliográficos
Autor(a) principal: Chaves,Otávio A.
Data de Publicação: 2018
Outros Autores: Echevarria,Áurea, Esteves-Souza,Andressa, Maciel,Maria A. M., Netto-Ferreira,José C.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Journal of the Brazilian Chemical Society (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532018000901786
Resumo: The interaction between HSA and two semi-synthetic potential anti-cancer agents derived from trans -dehydrocrotonin-methyl-hydrazone (MHDCTN) and phenyl-hydrazone (PHDCTN) was evaluated under physiological conditions at 296, 303 and 310 K by multi-spectroscopic techniques and molecular docking calculations. Steady state fluorescence quenching indicated a ground state association (static quenching) for both samples; however, the quenching induced by PHDCTN was not essentially static and can be accompanied by a dynamic quenching mechanism. The binding is strong (modified Stern-Volmer binding constant (Ka) ca. 105 M-1), causing a very weak perturbation on the secondary structure of the protein and there is just one main binding site for both samples (Sudlow’s site I). Molecular docking results suggested hydrogen bonding and hydrophobic interactions as the main binding forces for both samples.
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spelling In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic ClerodanesCroton cajucaratrans-dehydrocrotonin derivativeshuman serum albuminspectroscopymolecular dockingThe interaction between HSA and two semi-synthetic potential anti-cancer agents derived from trans -dehydrocrotonin-methyl-hydrazone (MHDCTN) and phenyl-hydrazone (PHDCTN) was evaluated under physiological conditions at 296, 303 and 310 K by multi-spectroscopic techniques and molecular docking calculations. Steady state fluorescence quenching indicated a ground state association (static quenching) for both samples; however, the quenching induced by PHDCTN was not essentially static and can be accompanied by a dynamic quenching mechanism. The binding is strong (modified Stern-Volmer binding constant (Ka) ca. 105 M-1), causing a very weak perturbation on the secondary structure of the protein and there is just one main binding site for both samples (Sudlow’s site I). Molecular docking results suggested hydrogen bonding and hydrophobic interactions as the main binding forces for both samples.Sociedade Brasileira de Química2018-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532018000901786Journal of the Brazilian Chemical Society v.29 n.9 2018reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.21577/0103-5053.20180054info:eu-repo/semantics/openAccessChaves,Otávio A.Echevarria,ÁureaEsteves-Souza,AndressaMaciel,Maria A. M.Netto-Ferreira,José C.eng2018-08-16T00:00:00Zoai:scielo:S0103-50532018000901786Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2018-08-16T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes
title In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes
spellingShingle In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes
Chaves,Otávio A.
Croton cajucara
trans-dehydrocrotonin derivatives
human serum albumin
spectroscopy
molecular docking
title_short In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes
title_full In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes
title_fullStr In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes
title_full_unstemmed In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes
title_sort In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes
author Chaves,Otávio A.
author_facet Chaves,Otávio A.
Echevarria,Áurea
Esteves-Souza,Andressa
Maciel,Maria A. M.
Netto-Ferreira,José C.
author_role author
author2 Echevarria,Áurea
Esteves-Souza,Andressa
Maciel,Maria A. M.
Netto-Ferreira,José C.
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Chaves,Otávio A.
Echevarria,Áurea
Esteves-Souza,Andressa
Maciel,Maria A. M.
Netto-Ferreira,José C.
dc.subject.por.fl_str_mv Croton cajucara
trans-dehydrocrotonin derivatives
human serum albumin
spectroscopy
molecular docking
topic Croton cajucara
trans-dehydrocrotonin derivatives
human serum albumin
spectroscopy
molecular docking
description The interaction between HSA and two semi-synthetic potential anti-cancer agents derived from trans -dehydrocrotonin-methyl-hydrazone (MHDCTN) and phenyl-hydrazone (PHDCTN) was evaluated under physiological conditions at 296, 303 and 310 K by multi-spectroscopic techniques and molecular docking calculations. Steady state fluorescence quenching indicated a ground state association (static quenching) for both samples; however, the quenching induced by PHDCTN was not essentially static and can be accompanied by a dynamic quenching mechanism. The binding is strong (modified Stern-Volmer binding constant (Ka) ca. 105 M-1), causing a very weak perturbation on the secondary structure of the protein and there is just one main binding site for both samples (Sudlow’s site I). Molecular docking results suggested hydrogen bonding and hydrophobic interactions as the main binding forces for both samples.
publishDate 2018
dc.date.none.fl_str_mv 2018-09-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532018000901786
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532018000901786
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.21577/0103-5053.20180054
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Química
publisher.none.fl_str_mv Sociedade Brasileira de Química
dc.source.none.fl_str_mv Journal of the Brazilian Chemical Society v.29 n.9 2018
reponame:Journal of the Brazilian Chemical Society (Online)
instname:Sociedade Brasileira de Química (SBQ)
instacron:SBQ
instname_str Sociedade Brasileira de Química (SBQ)
instacron_str SBQ
institution SBQ
reponame_str Journal of the Brazilian Chemical Society (Online)
collection Journal of the Brazilian Chemical Society (Online)
repository.name.fl_str_mv Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)
repository.mail.fl_str_mv ||office@jbcs.sbq.org.br
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