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Enzyme-Activatable Cell-Penetrating Peptides through a Minimal Side Chain Modification.
Bode, Saskia A; Hansen, Morten B; Oerlemans, Roy A J F; van Hest, Jan C M; Löwik, Dennis W P M.
Afiliação
  • Bode SA; Radboud University Nijmegen, Institute for Molecules and Materials, Bio-organic Chemistry, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
  • Hansen MB; Radboud University Nijmegen, Institute for Molecules and Materials, Bio-organic Chemistry, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
  • Oerlemans RA; Radboud University Nijmegen, Institute for Molecules and Materials, Bio-organic Chemistry, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
  • van Hest JC; Radboud University Nijmegen, Institute for Molecules and Materials, Bio-organic Chemistry, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
  • Löwik DW; Radboud University Nijmegen, Institute for Molecules and Materials, Bio-organic Chemistry, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
Bioconjug Chem ; 26(5): 850-6, 2015 May 20.
Article em En | MEDLINE | ID: mdl-25915685
Activatable cell-penetrating peptides are of great interest in drug delivery because of their enhanced selectivity which can be controlled by the external stimuli that trigger their activation. The use of a specific enzymatic reaction to trigger uptake of an inert peptide offers a relevant targeting strategy because the activation process takes place in a short time and only in areas where the specific cell surface enzyme is present. To this aim, the lysine side chain of Tat peptides was modified with an enzyme-cleavable domain of minimal size. This yielded blocked Tat-peptides which were inactive but that could be activated by coincubation with the selected enzymes.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dipeptidil Peptidases e Tripeptidil Peptidases / Peptídeos Penetradores de Células / Aminopeptidases Limite: Humans Idioma: En Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dipeptidil Peptidases e Tripeptidil Peptidases / Peptídeos Penetradores de Células / Aminopeptidases Limite: Humans Idioma: En Ano de publicação: 2015 Tipo de documento: Article