| Product Name | [Asn23]-Beta-Amyloid (1-40), D23N Iowa Mutation |
| Catalog Number | LT9152 |
| Product Quantity | 0.5 mg |
| Sequence | DAEFRHDSGYEVHHQKLVFFAENVGSNKGAIIGLMVGGVV |
| Mutation | D23N (Iowa) |
| Molecular Weight | 4329.2 |
| Purity | ≥95% |
| Mechanism & Biological Significance | The Iowa D23N mutation removes the Asp23 negative charge in Aβ40 and is strongly associated with cerebral amyloid angiopathy. The mutation promotes rapid fibril formation and can stabilize fibril architectures distinct from wild-type Aβ40. |
| Published Research Context | Exact D23N-Aβ40 has been synthesized and studied by electron microscopy, X-ray diffraction and solid-state NMR. Published work reports markedly faster fibril formation than wild-type Aβ40 and documents parallel and antiparallel β-sheet architectures. |
| Research Applications | - Iowa mutation and cerebral amyloid angiopathy research
- Aβ40 fibril kinetics
- solid-state NMR and fibril-structure studies
- seeded growth and polymorphism studies
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| Experimental Considerations | The mutation and the Aβ40 C-terminal boundary are integral to this construct. Wild-type and mutant peptides should be prepared with matched dissolution, concentration, incubation, buffer and aggregation protocols because Aβ assembly is strongly preparation-dependent. |
| Selected Scientific References | - Evidence for novel beta-sheet structures in Iowa mutant beta-amyloid fibrils
- Structural evolution of Iowa-mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth
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