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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
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Biochemistry
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JoVE Journal Biochemistry
Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

DOI:
10.3791/63495-v

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09:39 min

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March 31, 2022

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, , , ,
1The Azrieli Faculty of Medicine in the Galilee,Bar-Ilan University, 2Asian Liver Center, Department of Surgery,Stanford University School of Medicine

Chapters

  • 00:04Introduction
  • 01:16Chip Activation
  • 02:09Target Protein Immobilization
  • 03:09Preparing Analyte Samples and Running the Experiment
  • 06:09Analysis
  • 06:43Results: Data Files Generated from Hsp90 and Cdc37 Interaction Using FEB System (Experiment 1 and 2) and ITC Analysis
  • 08:39Conclusion

Summary

Automatic Translation

Automatic Translation

Field-effect biosensing (FEB) is a label-free technique for detecting biomolecular interactions. It measures the electric current through the graphene biosensor to which the binding targets are immobilized. The FEB technology was used to evaluate biomolecular interactions between Hsp90 and Cdc37 and a strong interaction between the two proteins was detected.

Tags

Keywords: Biomolecular InteractionMolecular Chaperone Hsp90Client Protein Kinase Cdc37Field-effect Biosensing TechnologyFEBLabel-freeCost-effectiveInteraction DetectionInhibitor TestingAutomatedUser-friendlyPharmaceuticalsBiomolecular AnalysisDrug ValidationChip FunctionalizationEDCSulfo-NHSMES BufferPBSTarget MoleculeQuench Solution

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