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Beta-Amyloid (31-40), sequence IIGLMVGGVV, is a highly hydrophobic C-terminal fragment derived from the amyloid-β peptide associated with Alzheimer’s disease research. This segment corresponds to a portion of the transmembrane-facing hydrophobic domain of amyloid-β and plays an important role in peptide self-association, membrane interaction, and aggregation behavior.
The sequence contains multiple hydrophobic residues, including isoleucine, leucine, methionine, and valine, which contribute strongly to intermolecular interactions and amyloid assembly. Because of these physicochemical properties, the IIGLMVGGVV fragment is commonly used in studies examining amyloid aggregation, fibril nucleation, membrane insertion, and peptide secondary structure formation.
Research Background
The C-terminal hydrophobic region of amyloid-β is widely recognized as a major contributor to aggregation propensity and neurotoxic oligomer formation. Compared with N-terminal amyloid fragments, the C-terminal domain demonstrates significantly stronger hydrophobic interactions and plays a central role in stabilizing amyloid fibrils and oligomeric assemblies.
The IIGLMVGGVV fragment represents one of the most aggregation-prone regions within amyloid-β and has therefore been used as a simplified model system for studying hydrophobic peptide-driven self-assembly. Researchers frequently employ this fragment in biophysical studies to investigate amyloid nucleation mechanisms and peptide–membrane interactions without the complexity of the full-length peptide.
Applications in Alzheimer’s Disease and Amyloid Research
- Amyloid aggregation and fibrillation studies
- Hydrophobic peptide self-assembly research
- Membrane interaction and insertion analysis
- Secondary structure and β-sheet formation studies
- Oligomerization and fibril nucleation assays
- Biophysical characterization of amyloid domains
Membrane Interaction Studies
Because the IIGLMVGGVV sequence is strongly hydrophobic, it is frequently used in studies involving peptide–lipid interactions and membrane perturbation. The fragment has been investigated in model membrane systems, lipid vesicles, and bilayer studies to understand how amyloid peptides associate with cellular membranes and potentially contribute to membrane destabilization.
Hydrophobic amyloid segments such as IIGLMVGGVV are also relevant to studies examining peptide insertion into membrane-like environments and the formation of aggregation-prone conformations under physiologically relevant conditions.
Aggregation and Structural Studies
The peptide is useful for structural studies involving amyloidogenic peptides because its hydrophobic character strongly favors intermolecular association and β-sheet-rich assemblies. Researchers commonly analyze this fragment using circular dichroism (CD), NMR, FTIR, fluorescence spectroscopy, and electron microscopy techniques.
This fragment may also serve as a model sequence for investigating how small molecules, metals, surfactants, or peptide modifications influence amyloid aggregation behavior.
Why Use Aβ (31-40)?
- Represents a key hydrophobic region of amyloid-β
- Strong aggregation and self-assembly behavior
- Useful for membrane interaction studies
- Relevant to amyloid fibril and oligomer formation research
- Simplified model system for hydrophobic amyloid domains
Solubility and Handling Notes
Due to its highly hydrophobic nature, IIGLMVGGVV may exhibit limited aqueous solubility and aggregation tendency. Researchers often dissolve the peptide in DMSO, HFIP, or other suitable organic solvents prior to dilution into aqueous buffers depending on the intended experimental protocol.
For additional information on amyloid peptide handling and solubilization strategies, please see:
Amyloid Peptides for Alzheimer’s Disease Research
Peptide Solubilization – Amyloids Case Study (PDF)
Related Products
Beta-Amyloid (1-42), human
Beta-Amyloid (1-40), Ultra Pure, TFA
Amyloid peptide category
Amyloid Peptides for Alzheimer’s Disease Research
Research Use Only. Not for human or therapeutic use.
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