Oligomer Formation
Oligomer Formation - Related Videos
06:34
A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
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Cited by 6 •
2017
Herein we report a tailored HPLC purification protocol that yields high-purity amyloid beta 42 (Aβ42) and amyloid beta 40 (Aβ40) peptides, capable of oligomer formation. Amyloid beta is a highly aggregation prone, hydrophobic peptide implicated in Alzheimer's disease. The amyloidogenic nature of the peptide makes its purification a challenge.
04:19
Size-Exclusion Chromatography with Multi-Angle Light Scattering for Protein Oligomers
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2025
This video describes SEC-MALS, which leverages the abilities of size-exclusion chromatography (SEC) and multi-angle light scattering (MALS). In SEC-MALS, the SEC separates proteins or protein complexes based on their size, and the MALS detector determines the average molecular weight by measuring the intensity of the light scattered by the molecule at different angles.
05:29
Controlled Infusion of Aβ Peptide-Specific Antibodies and Aβ Oligomers into the Rat Hippocampus
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2025
This video demonstrates a technique for the continuous infusion of amyloid-beta (Aβ) peptide-specific antibodies into the hippocampus of a rat. The study employs implanting a bilateral cannula system for a controlled infusion of Aβ peptide-specific antibodies coupled with the infusion of soluble Aβ oligomers (Aβo) into the rat hippocampus to study the interactions between the oligomers and the antibodies.
10:19
Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps
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Cited by 11 •
2016
To study the effects of Aβo in vivo, we developed a model based on repeated hippocampal infusions of soluble Aβo coupled with continuous infusion of Aβo antibody (6E10) in the hippocampus using osmotic pumps to counteract the neurotoxic effect of Aβo.
02:16
Solution Formation
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2020
There is no one solvent that can dissolve every type of solute. Some substances that readily dissolve in a certain solvent might be insoluble in a different solvent. A simple way to predict which substances dissolve in which solvent is the phrase "like dissolves like". This means that polar substances, such as salt and sugar, dissolve in a polar substance like water. In contrast, non-polar substances are more soluble in non-polar solvents such as carbon tetrachloride. This selective solubility...
FAQs
Assembly becomes more likely when subunits are sufficiently concentrated and have complementary, high-affinity interaction surfaces. These factors can determine whether association starts, continues cooperatively, or remains reversible. Consequently, changing concentration or interaction strength may shift a system between predominantly separate subunits and more persistent complexes, affecting the biological activity and stability of the resulting assembly.
A conformational change can expose, conceal, or reshape the surfaces that subunits use to associate. This may promote assembly, interrupt existing contacts, or change how the completed complex interacts with other molecules. Because oligomer formation can influence localization, signaling, and activity, structural rearrangements provide a mechanism for linking molecular state to downstream biological effects.
Several interaction types can support assembly, including hydrogen bonds, electrostatic forces, hydrophobic effects, and covalent cross-links. Their relative contribution depends on the complementary surfaces and chemical environment of the subunits. Noncovalent interactions can permit reversible association, whereas covalent cross-links can provide stronger stabilization, helping explain differences in persistence and functional behavior among complexes.
In immunology and infection, assembly can create multivalent structures that bind more effectively, amplify signaling, disrupt membranes, or support particle formation. Immune receptors and inflammasomes illustrate signaling-related roles, while viral proteins and microbial toxins illustrate pathogen-associated functions. Examining these assemblies therefore connects molecular organization with host defense, microbial damage, and disease mechanisms.
Characterization should address the number of associated subunits, the stability of the complex, and whether association is reversible. Researchers should also consider molecular affinity, concentration dependence, conformational changes, and the interaction forces supporting assembly. Relating these features to activity, localization, or signaling can reveal whether a complex is functionally important rather than merely structurally detectable.
This approach is particularly useful when a biological effect depends on coordinated subunits rather than isolated molecules. Investigating receptor assemblies, inflammasomes, viral protein complexes, or microbial toxin structures can clarify how multivalent binding, signal amplification, membrane disruption, or particle assembly occurs. The resulting mechanistic insight may support efforts to block harmful assemblies or stabilize beneficial molecular structures.