Novel terbium-sensitizing peptide substrates for cyclin-dependent kinase 5 (CDK5) and their demonstration in luminescence kinase assays

Jason L. Heier; Dylan J. Boselli; Laurie L Parker

doi:10.1039/d5cb00189g

Novel terbium-sensitizing peptide substrates for cyclin-dependent kinase 5 (CDK5) and their demonstration in luminescence kinase assays

Jason L. Heier, Dylan J. Boselli, Laurie L Parker

Biochemistry, Molecular Biology, and Biophysics (CBS)

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

Abstract

Novel time-resolved terbium luminescence assays were developed for CDK5 and CDK2 by designing synthetic substrates which incorporate phospho-inducible terbium sensitizing motifs with kinase substrate consensus sequences. A substrate designed for CDK5 showed no phosphorylation by CDK2, opening the possibility for CDK5-specific assay development for selective drug discovery.

Original language	English (US)
Journal	RSC Chemical Biology
DOIs	https://doi.org/10.1039/d5cb00189g
State	Accepted/In press - 2025

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© 2025 RSC.

PubMed: MeSH publication types

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10.1039/d5cb00189g

Cite this

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title = "Novel terbium-sensitizing peptide substrates for cyclin-dependent kinase 5 (CDK5) and their demonstration in luminescence kinase assays",

abstract = "Novel time-resolved terbium luminescence assays were developed for CDK5 and CDK2 by designing synthetic substrates which incorporate phospho-inducible terbium sensitizing motifs with kinase substrate consensus sequences. A substrate designed for CDK5 showed no phosphorylation by CDK2, opening the possibility for CDK5-specific assay development for selective drug discovery.",

author = "Heier, \{Jason L.\} and Boselli, \{Dylan J.\} and Parker, \{Laurie L\}",

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year = "2025",

doi = "10.1039/d5cb00189g",

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journal = "RSC Chemical Biology",

issn = "2633-0679",

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AU - Boselli, Dylan J.

AU - Parker, Laurie L

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AB - Novel time-resolved terbium luminescence assays were developed for CDK5 and CDK2 by designing synthetic substrates which incorporate phospho-inducible terbium sensitizing motifs with kinase substrate consensus sequences. A substrate designed for CDK5 showed no phosphorylation by CDK2, opening the possibility for CDK5-specific assay development for selective drug discovery.

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SN - 2633-0679

JO - RSC Chemical Biology

JF - RSC Chemical Biology

ER -

Novel terbium-sensitizing peptide substrates for cyclin-dependent kinase 5 (CDK5) and their demonstration in luminescence kinase assays

Abstract

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