Enzyme-activatable cell-penetrating peptides through a minimal side chain modification

S.A. Bode, M.B. Hansen, R.A.J.F. Oerlemans, J.C.M. van Hest, D.W.P.M. Löwik

Research output: Contribution to journalArticleAcademicpeer-review

22 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)850-856
Number of pages7
JournalBioconjugate Chemistry
Issue number5
Publication statusPublished - 20 May 2015
Externally publishedYes


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