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Developing Selective-Dissociation for Proteoform Characterization in Top-Down Proteomics

Award Number: R01GM158899
ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)
PERIOD OF PERFORMANCE START DATE: 03/15/2026
PERIOD OF PERFORMANCE END DATE: 02/28/2030

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Developing Selective-Dissociation for Proteoform Characterization in Top-Down Proteomics - Summary This project seeks to develop enabling technology for the characterization of all human proteoforms. Proteoforms are the active species in biology and include not just the genetically encoded protein sequence but any alterations including alternate splicing, post-translational modifications, spontaneous chemical modifications, etc. As such their structure cannot be readily inferred from genomic data. Identification and characterization of proteoforms is the first step towards developing a complete mechanistic understanding of the cellular processes underlying both health and disease. Proteoforms are large, complex molecules that can be difficult to disambiguate. For example, an important functional difference could result from changing the location of a single modification, creating isomers that would appear to be nearly identical in an analytical sense. However, differences in key areas would distinguish these two proteoforms, and this proposal will develop methods to target those key differences by rationally and specifically fragmenting proteoforms at desired residues inside a mass spectrometer. This approach is an improvement over existing methods where information content is dependent on random fragmentation events, which may or may not reveal the key areas that differ. To enable rational protein dissection in the gas phase, chemical modifications must first be installed to create a weak link in the backbone chain that can be specifically triggered. The proposal will develop novel photoactivated modifiers that will selectively create radicals that will facilitate selective dissociation. Both the synthetic modifications and subsequent mass spectrometry are crucial innovations that will result from this research and further advance our ability to characterize proteoforms with the end goal of populating a human proteoform atlas.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2026 ( Subtotal = $396,886 )
2026	2026	REGENTS OF THE UNIVERSITY OF CALIFORNIA AT RIVERSIDE	200 UNIVERSTY OFC BUILDING	RIVERSIDE	CA	92521	RIVERSIDE	USA	Biomedical Research and Research Training	000	1	3/13/2026	NEW	$396,886
														Subtotal = $396,886

Grand Total All Awards = $396,886

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Developing Selective-Dissociation for Proteoform Characterization in Top-Down Proteomics

Award Number: R01GM158899

ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

PERIOD OF PERFORMANCE START DATE: 03/15/2026

PERIOD OF PERFORMANCE END DATE: 02/28/2030

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