An Inducible Reconstitution and Real-time Quantitative Kinetic System for the Analysis of Catalysis and Inhibition in Membranes

Case ID:
C12181
Disclosure Date:
10/1/2012

C12181: An assay to evaluate membrane-immersed enzyme kinetics in real time.

Novelty:

This technology is an inducible and real-time quantitative kinetic assay for the analysis of intra-membrane proteolysis.

Value Proposition:

Intra-membrane proteases can catalyze hydrolysis immersed within membranes. These enzymes are implicated in diseases such as Alzheimers disease, Parkinsons disease, Malaria and Tuberculosis. No assay is currently available to quantitatively monitor catalysis occurring within a cells natural membrane setting in real-time. This invention provides a novel assay for the analysis of intra-membrane proteolysis. Advantages of this technology include:

• Inducible reconstitution, which prevents premature catalysis and keeps the enzyme in an off state until needed.
• Real time analysis can be performed by using a fluorogenic substrate which is naturally quenched into the membrane. Active enzyme can release a fluorescent signal that is easily measured.
• This assay has been tested using Rhomboid enzymes and can be applied to other membrane-immersed protease.
• This assay can be miniaturized or used in high-throughput settings.
JAHXXX

Looking for Partners:

This technology can be made into a kit to assess enzyme activity. This technology can be implemented in robust next generation high-throughput screens with enzymes that perform catalysis inside the membrane bilayer.

Stage of Development:

Discovery

Data Availability:

Published paper

Publications/Associated Cases:

Cell. 2013 Dec 5;155(6):1270-81.

Patent Information:
Title App Type Country Serial No. Patent No. File Date Issued Date Expire Date Patent Status
An Inducible Reconstitution and Real-time Quantitative Kinetic System for the Analysis of Catalysis and Inhibition in Membranes PCT: Patent Cooperation Treaty United States 14/436,139 10,030,260 4/16/2015 7/24/2018 5/9/2033 Granted
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For Information, Contact:
Mark Maloney
dmalon11@jhu.edu
410-614-0300
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