"Zipper" molecular beacons : A generalized strategy to optimize the performance of activatable protease probes

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journal

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Author(s)

  • Juan Chen
  • Tracy W. B. Liu
  • Pui-Chi Lo
  • Brian C. Wilson
  • Gang Zheng

Detail(s)

Original languageEnglish
Pages (from-to)1836-1842
Journal / PublicationBioconjugate Chemistry
Volume20
Issue number10
Publication statusPublished - 21 Oct 2009
Externally publishedYes

Abstract

We report the proof-of-principle concept for zipper molecular beacons (ZMB) comprising an asymmetrical polyarginine/polyglutamate electrostatic "zipper" hairpin-linked fluorophore-quencher pair. The objective is to balance maximal quenching efficiency and optimal two-step activation (protease cleavage/zipper dissociation), while enhancing target cell uptake. This strategy also eliminates the peptide sequence dependence of conventional protease beacons. This ZMB concept is a generalizable approach to improve the functionality of a wide range of diagnostic/therapeutic probes through a simple switching of substrate sequences. © 2009 American Chemical Society.

Citation Format(s)

"Zipper" molecular beacons : A generalized strategy to optimize the performance of activatable protease probes. / Chen, Juan; Liu, Tracy W. B.; Lo, Pui-Chi; Wilson, Brian C.; Zheng, Gang.

In: Bioconjugate Chemistry, Vol. 20, No. 10, 21.10.2009, p. 1836-1842.

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journal