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Developing gel-based platform for quantitative phosphoproteomics

Award Information
Agency: Department of Health and Human Services
Branch: National Institutes of Health
Contract: 1R43GM116373-01
Agency Tracking Number: R43GM116373
Amount: $150,000.00
Phase: Phase I
Program: SBIR
Solicitation Topic Code: 100
Solicitation Number: PA14-071
Timeline
Solicitation Year: 2015
Award Year: 2015
Award Start Date (Proposal Award Date): 2015-09-01
Award End Date (Contract End Date): 2017-02-28
Small Business Information
3495 Kent Ave, Suite E400
West Lafayette, IN 47906-4182
United States
DUNS: 965433258
HUBZone Owned: No
Woman Owned: No
Socially and Economically Disadvantaged: No
Principal Investigator
 ANTON ILIUK
 (765) 490-6834
 anton.iliuk@tymora-analytical.com
Business Contact
 ANTON ILIUK
Phone: (765) 490-6834
Email: anton.iliuk@tymora-analytical.com
Research Institution
N/A
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 mass spectrometry has become an exceptionally useful tool for phosphoproteome analyses extensive experiments are very labor intensive and cost prohibitive to most researchers As a result despite many large scale phosphoproteomic studies the critical need for a routine and effective analysis of relevant phosphoproteins has not been addressed Through this NIH SBIR Phase I study we will develop a novel strategy for gel based phosphoproteome analysis called Difference Gel Electrophoresis of Phosphoproteome DiGEP and translate it into commercial products for simpler phosphorylation discovery assays The novel design will take advantage of the small molecule platform functionalized with titanium ions for selective binding to phosphoproteins and a UV based crosslinker to immobilize the reagent onto the bound phosphoprotein In addition two different but structurally similar fluorophores will be used to differentiate the phosphoproteome profiles of two samples ran on a single gel The strategy will allow quantitative measurements of phosphorylation between the two samples and will pin point which contrasted phosphoproteins should be further analyzed by mass spectrometry The proposed approach offers the promise of significant cost reduction and is fully compatible with gel systems and imaging software already developed for Difference Gel Electrophoresis DIGE

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. *

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