![[Asn23]-beta-Amyloid (1-42) Iowa Mutation](/uploads/48442/asn23-beta-amyloid-1-42-iowa-mutation20082.jpg)
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| Description | Introduces Iowa D23N onto Aβ42, disrupting the Asp23-Lys28 salt bridge and shifting conformation toward vascular deposition; used to study D23N effects on fibril polymorphism and pathology. |
Product Basic Information Table
| Standard English Name | Abbreviations/Aliases | Functional Tags | Structural Core | Molecular Formula | Exact MW (Da) | Average MW (Da) | Salt Form | Length (aa) |
| [Asn23]-Amyloid β-Protein (1-42) (Iowa mutation) | Aβ1-42 Iowa; D23N-Aβ42; APP D694N | Alzheimer's disease model peptide, familial mutant, cerebral amyloid angiopathy (CAA), oligomerization, vascular deposition, aggregation study | Full-length 42-mer, sequence DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVVIA; position 23 Asp→Asn (D23N; APP D694N Iowa mutation), removing the Asp23 negative charge and disrupting the E22-D23 intramolecular salt bridge; free N-terminus and C-terminus; C-terminal hydrophobic GVVIA drives strong β-sheet oligomer/fiber aggregation. | C203H312N56O59S | 4510.29 | 4513.12 | TFA salt / powder | 42 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Stability |
| PEP-ABN23-01 | White to off-white powder | -20°C, sealed, dry, light-protected, aliquots; ~2 years. Met-containing peptides require inert-gas (Ar/N2) headspace to prevent oxidation | 2-8°C for ~1 week; working aliquots stored at -20°C, avoid repeated freeze-thaw | Highly aggregating full-length 42-mer. Must be pre-treated with HFIP (hexafluoroisopropanol) to disaggregate, sonicated and centrifuged to isolate monomeric supernatant before dilution into PBS/buffer; do not reconstitute directly in aqueous buffer, which causes heterogeneous pre-aggregation. | solid stable ~2 years at -20°C, dry and sealed; equilibrate vial to RT in a desiccator before opening to avoid moisture uptake |
Functional Description
| Product Code | Short Summary (listing) | Detailed Biological Function | Research Areas | Targets/Receptors |
| PEP-ABN23-01 | Aβ1-42 Iowa mutant (D23N / APP D694N): removes the Asp23 negative charge and disrupts the E22-D23 salt bridge, markedly accelerating oligomerization and favoring cerebrovascular wall deposition. A key full-length model peptide for cerebral amyloid angiopathy (CAA) and early-onset familial AD; HFIP pre-treatment required. | The Iowa mutation (D23N, corresponding to APP D694N in the transmembrane region) is a familial variant associated with autosomal-dominant cerebral amyloid angiopathy (CAA) and early-onset Alzheimer's disease. Replacing the negatively charged Asp23 with neutral Asn eliminates the negative charge at position 23 and breaks the E22-D23 intramolecular salt bridge present in wild-type Aβ, shifting the conformational equilibrium toward β-sheet and strongly accelerating oligomer and fibril formation. Compared with wild-type Aβ42, the Iowa mutant aggregates faster and deposits preferentially in the leptomeningeal and cortical small-artery walls, causing wall thickening, fibrinoid necrosis and intracerebral hemorrhage rather than purely parenchymal plaques. This product is the full-length 42-mer retaining the hydrophobic C-terminal GVVIA aggregation core, suitable for: in vitro aggregation kinetics (ThT fluorescence), oligomer/fiber morphology (TEM/AFM), interaction with vascular endothelial and smooth-muscle cells, neurotoxicity assays (primary neurons/cell lines), screening of anti-aggregation compounds and anti-Aβ antibodies, and CAA mechanistic studies. HFIP pre-treatment to obtain a homogeneous monomeric starting state is recommended for batch-to-batch reproducibility. | Alzheimer's disease (AD) pathogenesis, cerebral amyloid angiopathy (CAA), familial mutant studies, protein aggregation & fibrillization, oligomer neurotoxicity, anti-aggregation drug screening, anti-Aβ antibody development | Aβ oligomers/fibrils; cerebrovascular wall (endothelium/smooth muscle); E22-D23 salt-bridge conformational epitopes |
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