Abeta Multimers
Abeta Multimers - Related Videos
10:48
SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval
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Cited by 26 •
2010
We describe a technique for the preparation of clarified human cortical homogenates, protein separation by SDS-PAGE, antigen retrieval and immunoblotting with an antibody to the Aβ peptide. Using this protocol, we consistently detect monomeric and multimeric Aβ in cortical tissue from humans with Alzheimer's pathology.
07:40
Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples
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2017
A method for stabilizing and separating native protein complexes from unmodified tissue lysate using an amine-reactive protein cross-linker coupled to a novel two-dimensional polyacrylamide gel electrophoresis (PAGE) system is presented.
06:59
Multimer-PAGE for Separating Native Protein Complexes: A Hybrid Separation Technique Consisting of Blue Native-PAGE and SDS-PAGE to Separate Intact Multimeric Proteins From Tissue Lysate
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2025
This video describes multimeric PAGE for separating native protein complexes from tissue homogenates. The technique is a hybrid of blue native-PAGE and SDS-PAGE techniques. The separated complexes can be characterized and studied for their role in cell functioning.
08:16
Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus
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Cited by 41 •
2015
Here, we present a protocol for direct stereotaxic brain infusion of amyloid-beta. This methodology provides an alternative in vivo mouse model to address the short-term effects of amyloid-beta on brain neurons.
11:57
Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase
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2025
Here, we describe a yeast system reconstituting human γ-secretase. This system allows for the identification and study of mutations affecting activity and for screening of γ-secretase inhibitors (GSIs). Utilizing the loss of function properties of familial Alzheimer's disease mutants, it is possible to screen for γ-secretase modulators (GSMs).
FAQs
Peptide-peptide interactions can change the conformation, or structural arrangement, of individual amyloid-beta molecules as they associate. These conformational changes influence whether assemblies progress toward oligomers, protofibrils, or fibrils. Because each form may have different stability and biological activity, following structural changes is essential for determining how assembly relates to effects on neuronal function.
Soluble and insoluble forms can differ in stability, distribution, and biological activity, so they may not produce identical effects in neural systems. Examining these properties separately helps researchers avoid treating all amyloid-beta assemblies as equivalent. This distinction is important when relating particular multimer populations to synaptic signaling, neuronal function, or cellular homeostasis.
Oligomers, protofibrils, and fibrils represent progressively larger assembly states formed during amyloid-beta association. Their different sizes and structural states provide a framework for comparing stability, distribution, and biological activity. In neuroscience research, this comparison helps identify whether specific stages of assembly are more closely associated with disrupted synaptic signaling or impaired neuronal function.
Not every amyloid-beta assembly necessarily has the same biological effect. Determining which multimer forms are associated with synaptic disruption, altered neuronal function, or loss of cellular homeostasis allows researchers to connect molecular assembly with neurotoxicity. That distinction supports more precise investigation of disease mechanisms and helps focus therapeutic strategies on relevant peptide forms rather than on amyloid-beta broadly.
Studies can focus on detecting and characterizing the different amyloid-beta assembly states, including oligomers, protofibrils, fibrils, and larger soluble or insoluble complexes. Researchers compare their properties, such as stability, distribution, and biological activity, to determine how each form relates to neural effects. These analyses provide evidence for linking particular assemblies with synaptic or cellular outcomes.
Characterizing assembly states enables researchers to evaluate strategies that target amyloid-beta association or the formation of particular multimer populations. The resulting comparisons can show whether altering assembly is relevant to effects on synaptic signaling, neuronal function, or cellular homeostasis. This approach keeps therapeutic evaluation connected to both molecular forms and their observed biological consequences in neuroscience.