Mechanistic Investigations into ADRD Associated Protein Structures in Biological Settings (R01 - Clinical Trial Not Allowed)

Active
Yes
Status
Posted
Published Date
June 5th, 2024
Close Date
October 4th, 2024
Award Ceiling
$500,000.00
Opportunity No.
PAR-24-234

Agency

National Institutes of Health (HHS-NIH11)

Eligible Applicants

Others

Funding Category

Health

Funding Instrument

Grant

Opportunity Category

Discretionary

Cost Sharing or Matching Requirement

Yes

Summary

The National Institutes of Health (NIH) has posted a grant opportunity titled "Mechanistic Investigations into ADRD Associated Protein Structures in Biological Settings (R01 - Clinical Trial Not Allowed)". This grant aims to support research on the structural biology of protein assemblies associated with Alzheimer's disease and related dementias (AD/ADRD) in their native cellular and tissue environments. The grant seeks to advance the understanding of protein structures and aggregates in AD/ADRD pathology, particularly focusing on the development of rational structure-based ligands for PET imaging. Currently, there is a lack of PET ligands that can specifically identify and monitor the accumulation of aggregated and misfolded proteins in AD/ADRD patients. The research should explore recent developments in structural biology that enable in situ characterization of macromolecular assemblies. By studying protein structures in their native environments, researchers can overcome limitations associated with ex-vivo samples and recombinant bacterial proteins. This approach has the potential to provide a more comprehensive understanding of the diversity of physiologically relevant protein species. The grant does not require cost sharing or matching and falls under the category of funding activity related to health. The maximum award ceiling for this grant is $500,000. The opportunity is open to various eligible applicants, including Alaska Native and Native Hawaiian Serving Institutions, Faith-based or Community-based Organizations, and Historically Black Colleges and Universities (HBCUs), among others. For more information and to apply, interested parties can visit the following website: http://grants.nih.gov/grants/guide/pa-files/PAR-24-234.html. Any further inquiries can be directed to NIH Grants Information at grantsinfo@nih.gov.

Description

Advances in structural biology have enabled the characterization of large protein assemblies that are linked to AD/ADRD pathology. However, most structural biology approaches require purified samples from cells and tissues or use recombinant bacterial proteins. The derived structures using ex-vivo material may not report the diversity of physiologically relevant species because reconstruction relies on class averaging that is biased towards dominant conformations that survive methodological processing. Recent developments in structural biology offer the possibility of in situ characterization of specific macromolecular assemblies. Structural information of protein assemblies and aggregates in their native cellular and tissue environments could facilitate rational structure-based ligand development. Currently, PET ligands that specifically identify and monitor the accumulation of aggregated and misfolded proteins in AD/ADRD patients are lacking.

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