# Shared resource to develop tools and reagents to study structural polymorphisms in Abeta amyloid aggregates in AD

> **NIH NIH U24** · UNIVERSITY OF CALIFORNIA-IRVINE · 2023 · $1,089,558

## Abstract

Project Abstract
Alzheimer’s disease (AD) is currently an incurable neurodegenerative disease that affects over 35 million people
worldwide, including 5.4 million individuals in the USA with a new case diagnosed every minute. Amyloids occur
commonly as key pathological features in a wide variety of neurodegenerative diseases such as AD and despite
30 years of intensive research, important questions about the significance, mechanisms and role in pathogenesis
of amyloids remain unresolved. Because of the strong implication of amyloid Aß peptide in familial AD,
preparations of amyloid aggregates (oligomers, fibrils) have been featured in over 100,000 publications over the
past 30 years. In many cases, conflicting, contradictory and non-reproducible data obfuscate the underlying
mechanisms of pathogenesis. Advances in structural biology have established the structures of several distinct
types of amyloid, leading to the discovery that amyloid structures are highly polymorphic with the same protein
sequence adopting distinct beta sheet folds. Moreover, different structures seem to correlate with different
disease subtypes, indicating that structural variation plays a role in pathogenesis. This polymorphism and
structural heterogeneity may also underly the irreproducibility and conflicting results that have plagued amyloid
research. This suggests a critical need for well-characterized, standardized protocols for the preparation of
different types of amyloid Aß aggregates and reagents to authenticate these preparations and specifically identify
and quantify these polymorphs in vitro and in brain in order to support basic research to understand the roles
and mechanisms of amyloids in disease pathogenesis. Therefore, the overall goal of this resource initiative is
to establish a source network for the development of reagents and protocols for the production, standardization,
characterization, authentication of amyloid oligomers and fibrils and the dissemination of these materials to
investigators.

## Key facts

- **NIH application ID:** 10706566
- **Project number:** 5U24AG079683-02
- **Recipient organization:** UNIVERSITY OF CALIFORNIA-IRVINE
- **Principal Investigator:** Charles G. Glabe
- **Activity code:** U24 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2023
- **Award amount:** $1,089,558
- **Award type:** 5
- **Project period:** 2022-09-30 → 2027-05-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10706566

## Citation

> US National Institutes of Health, RePORTER application 10706566, Shared resource to develop tools and reagents to study structural polymorphisms in Abeta amyloid aggregates in AD (5U24AG079683-02). Retrieved via AI Analytics 2026-05-27 from https://api.ai-analytics.org/grant/nih/10706566. Licensed CC0.

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