Development of a Multi-analyte Biosensor Platform Based on Computationally-Designed Proteins

Award Information
Agency: Department of Homeland Security
Branch: N/A
Contract: NBCHC050062
Agency Tracking Number: 0412017
Amount: $750,000.00
Phase: Phase II
Program: SBIR
Awards Year: 2011
Solicitation Year: 2004
Solicitation Topic Code: H-SB04.1-002
Solicitation Number: FY04.1
Small Business Information
1024 S. Innovation Way, Stillwater, OK, 74074-1508
DUNS: 879735579
HUBZone Owned: N
Woman Owned: N
Socially and Economically Disadvantaged: N
Principal Investigator
 Edward Knobbe
 Principal Investigator
 (405) 372-9535
Business Contact
 Jim Luby
Title: Chief Operating Officer
Phone: (405) 372-9535
Research Institution
Current antibody- or enzyme-based chemical and biological sensors generally suffer from several disadvantages including involved development cycles, short shelf life, implementation difficulties, and no clear path for new receptor development. We propose an approach based on the use of computationally designed proteins (CDPs) as receptor scaffolds. Such scaffolds overcome many of the problems encountered with biosensors. Significantly, this approach is a general method that provides a path to rapid development of specific receptors. In Phase I, we demonstrated the ability of solutions of computationally designed proteins to display a fluorescent signal change upon ligand binding, we attached computationally designed proteins to solid surfaces, and we demonstrated that fluorescently tagged, immobilized phosphonate-binding proteins can display fluorescent signal change upon ligand binding. Thus, we are confident that continuation of this project will yield favorable results. Specifically, during Phase II, we will continue development of biosensors that incorporate engineered periplasmic binding proteins that recognize and report organophosphate mimics and hydrolysis products of well-known nerve agents. The primary goal will be incorporation of highly stable CDPs into a prototype device for the detection of hydrolysis products of sarin and soman. We will continue our collaboration with Dr. H.W. Hellinga at Duke University Medical Center.

* Information listed above is at the time of submission. *

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