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

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

doi:10.1021/bc900207k

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

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

Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review

49 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1836-1842
Journal	Bioconjugate Chemistry
Volume	20
Issue number	10
DOIs	https://doi.org/10.1021/bc900207k
Publication status	Published - 21 Oct 2009
Externally published	Yes

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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. {\textcopyright} 2009 American Chemical Society.",

author = "Juan Chen and Liu, {Tracy W. B.} and Pui-Chi Lo and Wilson, {Brian C.} and Gang Zheng",

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T2 - A generalized strategy to optimize the performance of activatable protease probes

AU - Chen, Juan

AU - Liu, Tracy W. B.

AU - Lo, Pui-Chi

AU - Wilson, Brian C.

AU - Zheng, Gang

PY - 2009/10/21

Y1 - 2009/10/21

N2 - 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.

AB - 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.

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DO - 10.1021/bc900207k

M3 - RGC 21 - Publication in refereed journal

C2 - 19754039

SN - 1043-1802

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SP - 1836

EP - 1842

JO - Bioconjugate Chemistry

JF - Bioconjugate Chemistry

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ER -

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

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