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Integrated Platform for Mass-Spectrometric Studies of Protein Structure

Award Information
Agency: Department of Health and Human Services
Branch: National Institutes of Health
Contract: 2R42GM121133-02
Agency Tracking Number: R42GM121133
Amount: $1,228,144.00
Phase: Phase II
Program: STTR
Solicitation Topic Code: 400
Solicitation Number: PA18-575
Solicitation Year: 2018
Award Year: 2020
Award Start Date (Proposal Award Date): 2020-02-01
Award End Date (Contract End Date): 2022-01-31
Small Business Information
San Carlos, CA 94070-2060
United States
DUNS: 967100921
HUBZone Owned: No
Woman Owned: No
Socially and Economically Disadvantaged: No
Principal Investigator
 (650) 412-4210
Business Contact
Phone: (650) 450-1029
Research Institution
SAINT LOUIS, MO 63130-4862
United States

 Nonprofit College or University

Technology for studying the higher order structure (HOS) and interactions of biomolecules is a
highlighted NIGMS SBIR/STTR research topic. Mass-spectrometric methods for studying
HOS include hydroxyl radical footprinting as well as chemical methods to covalently label
amino acid side-chain functional groups, and also hydrogen/deuterium exchange (HDX) on
protein backbone amides. These methods require only small amounts of not-necessarily-pure
material, and can study conformation and dynamics of proteins in solution with or without
ligands. Mass spectrometric methods are especially well suited to biopharma comparability
and epitope mapping studies. Currently, there is no software that can analyze mass
spectrometric data from both covalent labeling and HDX experiments, even though the two
methods both probe solvent accessibility and, if combined, would give finer resolution and
greater confidence. The outcome will be vendor-neutral commercial software with advanced
analytical and reporting capabilities that can handle both HDX and covalent labeling
The higher order structure (HOS) of biomolecules determines function, binding partners,
immune response, and safety and efficacy of therapeutics. Mass-spectrometric
methods for studying HOS include hydrogen/deuterium exchange and covalent labeling
experiments such as oxidative footprinting. The proposed project will result in unique
software to analyze all types of mass spectrometric data for HOS studies, and will find
use in both academic research and the biopharmaceutical industry.

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

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