Membrane-translocating peptides and toxins: from nature to bedside

Detalhes bibliográficos
Autor(a) principal: Rádis -Baptista,Gandhi
Data de Publicação: 2008
Outros Autores: Kerkis,Alexandre, Prieto -Silva,Álvaro Rossan, Hayashi,Mirian Akemi Furuie, Kerkis,Irina, Tetsuo,Yamane
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=S0103-50532008000200004
Resumo: Today, different functional classes of bioactive peptides and toxins isolated from diverse sources of living organisms are known. In medicine, these polypeptides present the potential to be used structurally unmodified or to serve as templates for molecular design of improved derivatives. Here, we refer to members of three classes of remarkable peptides and toxins that act at the cell membranes level and membrane trafficking systems: (i) the binary toxins (ii) the antimicrobial peptides and (iii) the cell penetrating peptides. Binary toxins have been genetically manipulated to generate specific immunotoxins, while antimicrobial peptides are in use as alternative agents against resistant microbes and tumor cells. Cell penetrating peptides have applications as diverse as cell transfection and transport of nanomaterials. Our group is dissecting the capacity of crotamine, a peptide from rattlesnake venom, to translocate cell membranes and use it as a delivery system in the transducing technology and molecular imaging.
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spelling Membrane-translocating peptides and toxins: from nature to bedsidecytolysinbinary toxinantimicrobial peptidecell-penetrating peptideanimal toxinnanobiotechnologyToday, different functional classes of bioactive peptides and toxins isolated from diverse sources of living organisms are known. In medicine, these polypeptides present the potential to be used structurally unmodified or to serve as templates for molecular design of improved derivatives. Here, we refer to members of three classes of remarkable peptides and toxins that act at the cell membranes level and membrane trafficking systems: (i) the binary toxins (ii) the antimicrobial peptides and (iii) the cell penetrating peptides. Binary toxins have been genetically manipulated to generate specific immunotoxins, while antimicrobial peptides are in use as alternative agents against resistant microbes and tumor cells. Cell penetrating peptides have applications as diverse as cell transfection and transport of nanomaterials. Our group is dissecting the capacity of crotamine, a peptide from rattlesnake venom, to translocate cell membranes and use it as a delivery system in the transducing technology and molecular imaging.Sociedade Brasileira de Química2008-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532008000200004Journal of the Brazilian Chemical Society v.19 n.2 2008reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0103-50532008000200004info:eu-repo/semantics/openAccessRádis -Baptista,GandhiKerkis,AlexandrePrieto -Silva,Álvaro RossanHayashi,Mirian Akemi FuruieKerkis,IrinaTetsuo,Yamaneeng2008-04-08T00:00:00Zoai:scielo:S0103-50532008000200004Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2008-04-08T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv Membrane-translocating peptides and toxins: from nature to bedside
title Membrane-translocating peptides and toxins: from nature to bedside
spellingShingle Membrane-translocating peptides and toxins: from nature to bedside
Rádis -Baptista,Gandhi
cytolysin
binary toxin
antimicrobial peptide
cell-penetrating peptide
animal toxin
nanobiotechnology
title_short Membrane-translocating peptides and toxins: from nature to bedside
title_full Membrane-translocating peptides and toxins: from nature to bedside
title_fullStr Membrane-translocating peptides and toxins: from nature to bedside
title_full_unstemmed Membrane-translocating peptides and toxins: from nature to bedside
title_sort Membrane-translocating peptides and toxins: from nature to bedside
author Rádis -Baptista,Gandhi
author_facet Rádis -Baptista,Gandhi
Kerkis,Alexandre
Prieto -Silva,Álvaro Rossan
Hayashi,Mirian Akemi Furuie
Kerkis,Irina
Tetsuo,Yamane
author_role author
author2 Kerkis,Alexandre
Prieto -Silva,Álvaro Rossan
Hayashi,Mirian Akemi Furuie
Kerkis,Irina
Tetsuo,Yamane
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Rádis -Baptista,Gandhi
Kerkis,Alexandre
Prieto -Silva,Álvaro Rossan
Hayashi,Mirian Akemi Furuie
Kerkis,Irina
Tetsuo,Yamane
dc.subject.por.fl_str_mv cytolysin
binary toxin
antimicrobial peptide
cell-penetrating peptide
animal toxin
nanobiotechnology
topic cytolysin
binary toxin
antimicrobial peptide
cell-penetrating peptide
animal toxin
nanobiotechnology
description Today, different functional classes of bioactive peptides and toxins isolated from diverse sources of living organisms are known. In medicine, these polypeptides present the potential to be used structurally unmodified or to serve as templates for molecular design of improved derivatives. Here, we refer to members of three classes of remarkable peptides and toxins that act at the cell membranes level and membrane trafficking systems: (i) the binary toxins (ii) the antimicrobial peptides and (iii) the cell penetrating peptides. Binary toxins have been genetically manipulated to generate specific immunotoxins, while antimicrobial peptides are in use as alternative agents against resistant microbes and tumor cells. Cell penetrating peptides have applications as diverse as cell transfection and transport of nanomaterials. Our group is dissecting the capacity of crotamine, a peptide from rattlesnake venom, to translocate cell membranes and use it as a delivery system in the transducing technology and molecular imaging.
publishDate 2008
dc.date.none.fl_str_mv 2008-01-01
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=S0103-50532008000200004
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532008000200004
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0103-50532008000200004
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.19 n.2 2008
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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