Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II

Detalhes bibliográficos
Autor(a) principal: FAUTH,EDSON V.F.
Data de Publicação: 2014
Outros Autores: CILLI,EDUARDO M., LIGABUE-BRAUN,RODRIGO, VERLI,HUGO
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Anais da Academia Brasileira de Ciências (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652014000401949
Resumo: Actinoporins are a family of pore-forming proteins with hemolytic activity. The structural basis for such activity appears to depend on their correct folding. Such folding encompasses a phosphocholine binding site, a tryptophan-rich region and the activity-related N-terminus segment. Additionally, different solution conditions are known to be able to influence the pore formation by actinoporins, as for Sticholysin II (StnII) and Equinatoxin II (EqtxII). In this context, the current work intends to characterize the influence of distinct solution conditions in the conformational behavior of these proteins through molecular dynamics (MD) simulations. The obtained data offer structural insights into actinoporins dynamics in solution, characterizing its conformational behavior at the atomic level, in accordance with previous experimental data on StnII and EqtxII hemolytic activities.
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spelling Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin IIActinoporinsGROMACSMolecular dynamicsPore-forming proteinsActinoporins are a family of pore-forming proteins with hemolytic activity. The structural basis for such activity appears to depend on their correct folding. Such folding encompasses a phosphocholine binding site, a tryptophan-rich region and the activity-related N-terminus segment. Additionally, different solution conditions are known to be able to influence the pore formation by actinoporins, as for Sticholysin II (StnII) and Equinatoxin II (EqtxII). In this context, the current work intends to characterize the influence of distinct solution conditions in the conformational behavior of these proteins through molecular dynamics (MD) simulations. The obtained data offer structural insights into actinoporins dynamics in solution, characterizing its conformational behavior at the atomic level, in accordance with previous experimental data on StnII and EqtxII hemolytic activities.Academia Brasileira de Ciências2014-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652014000401949Anais da Academia Brasileira de Ciências v.86 n.4 2014reponame:Anais da Academia Brasileira de Ciências (Online)instname:Academia Brasileira de Ciências (ABC)instacron:ABC10.1590/0001-3765201420140270info:eu-repo/semantics/openAccessFAUTH,EDSON V.F.CILLI,EDUARDO M.LIGABUE-BRAUN,RODRIGOVERLI,HUGOeng2015-10-27T00:00:00Zoai:scielo:S0001-37652014000401949Revistahttp://www.scielo.br/aabchttps://old.scielo.br/oai/scielo-oai.php||aabc@abc.org.br1678-26900001-3765opendoar:2015-10-27T00:00Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)false
dc.title.none.fl_str_mv Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II
title Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II
spellingShingle Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II
FAUTH,EDSON V.F.
Actinoporins
GROMACS
Molecular dynamics
Pore-forming proteins
title_short Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II
title_full Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II
title_fullStr Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II
title_full_unstemmed Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II
title_sort Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II
author FAUTH,EDSON V.F.
author_facet FAUTH,EDSON V.F.
CILLI,EDUARDO M.
LIGABUE-BRAUN,RODRIGO
VERLI,HUGO
author_role author
author2 CILLI,EDUARDO M.
LIGABUE-BRAUN,RODRIGO
VERLI,HUGO
author2_role author
author
author
dc.contributor.author.fl_str_mv FAUTH,EDSON V.F.
CILLI,EDUARDO M.
LIGABUE-BRAUN,RODRIGO
VERLI,HUGO
dc.subject.por.fl_str_mv Actinoporins
GROMACS
Molecular dynamics
Pore-forming proteins
topic Actinoporins
GROMACS
Molecular dynamics
Pore-forming proteins
description Actinoporins are a family of pore-forming proteins with hemolytic activity. The structural basis for such activity appears to depend on their correct folding. Such folding encompasses a phosphocholine binding site, a tryptophan-rich region and the activity-related N-terminus segment. Additionally, different solution conditions are known to be able to influence the pore formation by actinoporins, as for Sticholysin II (StnII) and Equinatoxin II (EqtxII). In this context, the current work intends to characterize the influence of distinct solution conditions in the conformational behavior of these proteins through molecular dynamics (MD) simulations. The obtained data offer structural insights into actinoporins dynamics in solution, characterizing its conformational behavior at the atomic level, in accordance with previous experimental data on StnII and EqtxII hemolytic activities.
publishDate 2014
dc.date.none.fl_str_mv 2014-12-01
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=S0001-37652014000401949
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652014000401949
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/0001-3765201420140270
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 Academia Brasileira de Ciências
publisher.none.fl_str_mv Academia Brasileira de Ciências
dc.source.none.fl_str_mv Anais da Academia Brasileira de Ciências v.86 n.4 2014
reponame:Anais da Academia Brasileira de Ciências (Online)
instname:Academia Brasileira de Ciências (ABC)
instacron:ABC
instname_str Academia Brasileira de Ciências (ABC)
instacron_str ABC
institution ABC
reponame_str Anais da Academia Brasileira de Ciências (Online)
collection Anais da Academia Brasileira de Ciências (Online)
repository.name.fl_str_mv Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)
repository.mail.fl_str_mv ||aabc@abc.org.br
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