Membrane-translocating peptides and toxins: from nature to bedside
Autor(a) principal: | |
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Data de Publicação: | 2008 |
Outros Autores: | , , , , |
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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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 |
_version_ |
1750318168603099136 |