Multiplexed detection and imaging of protein phosphorylation based on soluble nan

Award Information
Agency:
Department of Health and Human Services
Branch
n/a
Amount:
$147,515.00
Award Year:
2012
Program:
SBIR
Phase:
Phase I
Contract:
1R43EB015809-01
Agency Tracking Number:
R43EB015809
Solicitation Year:
2012
Solicitation Topic Code:
NIBIB
Solicitation Number:
PA11-096
Small Business Information
TYMORA ANALYTICAL OPERATIONS, LLC
1281 WIN HENTSCHEL BLVD, WEST LAFAYETTE, IN, -
Hubzone Owned:
N
Minority Owned:
N
Woman Owned:
N
Duns:
965433258
Principal Investigator:
ANTON ILIUK
(765) 430-1592
anton.iliuk@tymora-analytical.com
Business Contact:
VICKY TSENG
(765) 430-1592
vickyt@tymora-analytical.com
Research Institution:
Stub




Abstract
DESCRIPTION (provided by applicant): With recent technical advances, multiple important signaling pathways that may be the causes of human malignancy have continuously been discovered and dissected. The vast majority of these signaling pathways involve reversible protein phosphorylation, and the information on the location and dynamics of phosphorylation provides important mechanisms on how the signaling networks function and interact. While translational research gradually shifts from lab models to clinical samples, with the ultimate goal of identifying cancer biomarkers, a simple and reliable phosphorylation assay method is still missing for routine detection of phosphorylation in complex and typically heterogeneous clinical samples. Through this NIH SBIRPhase I study, we will further develop a novel strategy for phosphorylation assay, termed pIMAGO (phospho-imaging) that has recently been introduced by us, into commercial products for simple, routine phosphorylation assays. This novel design takes advantage of not only the quantum size properties of the soluble nanoparticles, but also of the multi-functionalized nature of the molecule, allowing for highly selective, sensitive and simple qualitative and quantitative assessment of protein phosphorylation without the use of either radioactive isotopes or expensive phosphospecific antibodies. Due to its size and unique properties, it also offers the capability for multiplexed detection of phosphorylation and total protein amount simultaneously. We propose to optimize the technology for on-membrane phosphoprotein detection in routine biomedical research. In addition, we will develop a novel fluorescence-based pIMAGO reagent for direct detection and multiplexed experiments to add another dimension for biomedicalresearch and development. PUBLIC HEALTH RELEVANCE: Protein phosphorylation relates to the onset and development of many cancer types and a highly efficient technology for phosphorylation analysis is critical for cancer research. This NIH SBIR will support an effort to develop an innovative technology into commercial products that equip researchers with powerful tools and new directions to combat the devastating disease.

* information listed above is at the time of submission.

Agency Micro-sites


SBA logo

Department of Agriculture logo

Department of Commerce logo

Department of Defense logo

Department of Education logo

Department of Energy logo

Department of Health and Human Services logo

Department of Homeland Security logo

Department of Transportation logo

Enviromental Protection Agency logo

National Aeronautics and Space Administration logo

National Science Foundation logo
US Flag An Official Website of the United States Government