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

Award Information
Agency:
Department of Homeland Security
Branch
n/a
Amount:
$750,000.00
Award Year:
2005
Program:
SBIR
Phase:
Phase II
Contract:
NBCHC050062
Award Id:
69248
Agency Tracking Number:
0412017
Solicitation Year:
2004
Solicitation Topic Code:
H-SB04.1-002
Solicitation Number:
n/a
Small Business Information
1024 S. Innovation Way, Stillwater, OK, 74074-
Hubzone Owned:
N
Minority Owned:
N
Woman Owned:
N
Duns:
879735579
Principal Investigator:
EdwardKnobbe
Senior Engineer
(405) 372-9535
eknobbe@nomadics.com
Business Contact:
JimLuby
Chief Operating Officer
(405) 372-9535
jluby@nomadics.com
Research Institute:
n/a
Abstract
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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