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Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays
Published on: October 23, 2019
A quantitative analysis of kinase inhibitor selectivity
Mazen W Karaman1, Sanna Herrgard, Daniel K Treiber
1Ambit Biosciences, 4215 Sorrento Valley Blvd., San Diego, California 92121, USA.
Nature Biotechnology
|January 10, 2008
Summary
This study maps interactions of 38 kinase inhibitors against over 300 human kinases. It reveals diverse interaction patterns and introduces a selectivity score, highlighting the limitations of small assay panels for robust selectivity measurement.
Area of Science:
- Pharmacology
- Biochemistry
- Drug Discovery
Background:
- Kinase inhibitors are a novel therapeutic class with potential for multi-target inhibition.
- The biological impact of multi-kinase activity remains poorly understood.
- Understanding kinase inhibitor selectivity is crucial for efficacy and safety.
Purpose of the Study:
- To explore kinase inhibitor interactions with the human kinome.
- To generate comprehensive interaction maps for 38 kinase inhibitors.
- To develop a method for quantifying kinase inhibitor selectivity.
Main Methods:
- Screening of 38 kinase inhibitors against a panel of 317 human kinases.
- Generation of interaction maps detailing inhibitor-kinase binding.
- Introduction and application of a selectivity score for data analysis.
Main Results:
- The study presents the most comprehensive kinase inhibitor selectivity data to date.
- Diverse and varied interaction patterns were observed across the kinome.
- A novel selectivity score was introduced to quantify inhibitor profiles.
- Small assay panels were found to be insufficient for accurate selectivity assessment.
Conclusions:
- Kinase inhibitor selectivity is highly diverse and complex.
- The developed selectivity score provides a valuable tool for analyzing inhibitor profiles.
- Comprehensive kinome-wide screening is essential for robust selectivity evaluation.
