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Quinolimide-based peptide biosensor for probing p25 in vitro and in living cells

  • Francisco Fueyo-González
  • , Rosario Herranz
  • , Simona Plesselova
  • , Maria D. Giron
  • , Rafael Salto
  • , Jose Manuel Paredes
  • , Angel Orte
  • , May C. Morris
  • , Juan A. González-Vera

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

CDK5 kinase is activated through interactions with different partners including the p35/p25 regulators. Active CDK5 plays a key role in several neuronal functions and its hyperactivity contributes to a variety of neurodegenerative processes and several human cancers, in particular glioblastomas and neuroblastomas. In order to probe partners that interact with CDK5, we designed and synthesized fluorescent quinolimide-labelled peptides derived from the C-helix of CDK5, which were implemented to probe CDK5 partners in vitro and by in cellulo imaging in U87 glioblastoma and N2a neuroblastoma cells. Ectopic expression of a NIR fluorescent protein miRFP670 fusion with p25 (p25-miRFP670) in N2a cells induced FRET between a quinolimide-labelled peptide biosensor and p25-miRFP670, and fluorescence intensity was proportional to the expression level of p25, thereby demonstrating the potential of the quinolimide-labelled peptide biosensor to report on p25 relative abundance.

Original languageEnglish
Article number129929
JournalSensors and Actuators, B: Chemical
Volume339
DOIs
StatePublished - 15 Jul 2021

Keywords

  • CDK5
  • FRET imaging
  • Fluorescence probes
  • Protein-protein interactions
  • Quinolimide derivatives
  • p25 sensors

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