Fast fragmentation method for characterization of peptides with labile PTMs

Award Information
Agency:
Department of Health and Human Services
Branch
n/a
Amount:
$413,605.00
Award Year:
2012
Program:
SBIR
Phase:
Phase I
Contract:
1R43GM103358-01
Award Id:
n/a
Agency Tracking Number:
R43GM103358
Solicitation Year:
2012
Solicitation Topic Code:
NIGMS
Solicitation Number:
PA11-215
Small Business Information
6992 COLUMBIA GATEWAY DR, #200, COLUMBIA, MD, -
Hubzone Owned:
N
Minority Owned:
Y
Woman Owned:
N
Duns:
123310083
Principal Investigator:
EUGENE MOSKOVETS
(443) 539-1710
moskovets@apmaldi.com
Business Contact:
ARNOLD LEE
(443) 539-1710
alee@apmaldi.com
Research Institution:
Stub




Abstract
DESCRIPTION (provided by applicant): Significant increase in the efficiency and speed of electron transfer dissociation (ETD) in tandem mass spectrometry (MS) will have a profound impact on its applications to the entire analytical field of characterization of posttranslational modifications (PTM) in proteins. At present, the applicability of ETD-based MS analysis as a unique analytical tool specifically targeting PTM is limited by its low speed and by inability of ETD to efficiently dissociate proteins orpeptides with low charge density. We plan to build a novel ETD ion source generating an energetic beam of negative ions to significantly improve efficiency and speed of PTM detection of both proteins and peptides. To demonstrate high rate of MS/MS analysisbased on ETD, we plan to utilize capabilities of house-built desktop FTMS instrument equipped with multi-electrode detection system, and record MS/MS mass spectra obtained from fast ETD process with high mass resolution and in a short time. PUBLIC HEALTH RELEVANCE: Utilizing complementary fragmentation methods is a broadly used approach in mass-spectrometry based analysis of complex protein mixtures providing reliable identification of posttranslation modifications in proteins. We plan to developa novel source providing fast fragmentation that will substantially improve and accelerate characterization of posttranslation modifications in proteins analyzed in tandem mass spectrometers. The source can be easily incorporated into a design of a varietyof tandem mass spectrometers. This will allow much better detection of disease-specific biomarkers from biological fluids or tissues.

* 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