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Updated: Jul 24, 2025

Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Published on: March 16, 2016

Two structurally defined Aβ polymorphs promote different pathological changes in susceptible mice.

Ruben Gomez-Gutierrez^1,2, Ujjayini Ghosh³, Wai-Ming Yau³

¹Department of Neurology, The University of Texas Health Science Center at Houston, Houston, TX, USA.

|July 10, 2023

Summary

This summary is machine-generated.

Different strains of misfolded amyloid-beta (Aβ) show distinct properties and induce unique pathologies in Alzheimer's disease models. Understanding these Aβ strains is crucial for disease mechanism insights.

Keywords:

amyloid-beta animal models prion protein conformation strains

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Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

Area of Science:

Neuroscience
Biochemistry
Pathology

Background:

Misfolded amyloid-beta (Aβ) aggregates are implicated in Alzheimer's disease (AD) progression.
The specific roles of Aβ polymorphic variants and conformational strains in AD pathogenesis remain incompletely understood.

Purpose of the Study:

To investigate the seeding properties and biological impact of two structurally defined synthetic misfolded Aβ strains (2F and 3F).
To elucidate how different Aβ strains contribute to AD pathology.

Main Methods:

In vitro biochemical assays assessing proteolysis resistance, dye binding, and seeding.
In vivo studies involving injection into a transgenic mouse model of AD.
Solid-state nuclear magnetic resonance (ssNMR) for structural analysis of induced aggregates.

Main Results:

The 2F and 3F Aβ strains exhibited distinct biochemical properties and in vitro seeding behaviors.
In vivo, these strains induced varying aggregation rates, plaque morphologies, brain region tropism, and Aβ peptide recruitment (Aβ40/Aβ42).
Differential microglial and astroglial responses were observed, and ssNMR confirmed distinct structures of induced aggregates.

Conclusions:

Structurally distinct Aβ polymorphs possess unique biological activities and pathological consequences.
This research provides atomic-level characterization of Aβ polymorphs, offering critical insights into their pathological significance in Alzheimer's disease.