Singlet Oxygen-Mediated Protein Proximity Assay

Award Information
Agency:
Department of Health and Human Services
Branch
n/a
Amount:
$110,000.00
Award Year:
2008
Program:
SBIR
Phase:
Phase I
Contract:
1R43CA134465-01
Award Id:
88949
Agency Tracking Number:
CA134465
Solicitation Year:
n/a
Solicitation Topic Code:
n/a
Solicitation Number:
n/a
Small Business Information
PERSCITUS BIOSCIENCES, LLC, 3587 ANDERSON ST, STE 104, MADISON, WI, 53704
Hubzone Owned:
N
Minority Owned:
N
Woman Owned:
N
Duns:
790953868
Principal Investigator:
() -
Business Contact:
() -
scthomas@tds.net
Research Institution:
n/a
Abstract
DESCRIPTION (provided by applicant): Perscitus Biosciences, LLC, is developing a novel protein proximity assay with broad applications to the pharmaceutical and biomedical community. Currently, there are no satisfactory approaches for examining large prote in complexes in an intact cell and identifying associated proteins that may be important in discerning function. Researchers determine from microarray and other studies that a protein may be implicated in a disease process, but are unable to determine what the function of that protein is within the cell. The protein proximity technology being developed by Perscitus allows for the selective tagging of proteins within a limited radius of the protein of interest. The approach utilizes an active oxygen species, singlet oxygen, created photochemically, that is capable of only limited diffusion from its site of creation. This diffusion distance closely approximates the size of a multimeric protein complex. Singlet oxygen reacts with neighboring proteins, creating a carbonyl group that can be utilized for protein detection, identification and purification. The approach is tunable and precisely initiated at the time of illumination. We are proposing a focused investigation of this protein proximity assay to demonstra te proof of concept that can be used in marketing this approach to pharmaceutical companies. We will initially examine the protein MDM2 because of its broad importance to cancer biology, and the existence of a number of known binding partners that will ser ve as positive controls in our proof of concept studies. The simplicity and scalability of this approach should make for a powerful proteomic method that will have broad applicability to biomedical and pharmaceutical investigators.

* information listed above is at the time of submission.

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