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Home Product Peptide Catalog Products Neurodegenerative Disease Research Peptides Amyloid β-Protein (1–43) | Human Aβ43 Research Peptide

DESCRIPTION

Amyloid β-Protein (1–43), commonly abbreviated Aβ43, is a 43-amino-acid amyloid-β species generated through APP processing.

Aβ43 contains one additional C-terminal threonine compared with Aβ42. Although this represents only a single-residue extension, C-terminal length is an important determinant of Aβ hydrophobicity, γ-secretase processing, self-assembly, and molecular recognition.

Product Information

PropertySpecification
Product NameAmyloid β-Protein (1–43)
SequenceDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAT
Length43 amino acids
Molecular FormulaC207H318N56O62S
Theoretical MW~4615.21 Da
Peptide TypeAPP-derived amyloid-β species
C-Terminal ResidueThr43
Research Areasγ-Secretase, APP processing, aggregation, Aβ length comparison

Aβ43 in γ-Secretase Processing

Aβ43 is associated with one of the major processive γ-secretase pathways:

Aβ49 → Aβ46 → Aβ43 → Aβ40

This gives Aβ43 a useful role in studies of γ-secretase processivity, presenilin function, and sequential C-terminal trimming.

It can also help researchers examine how relatively small differences at the C-terminus influence the physical properties of amyloid peptides.

Comparing Aβ40, Aβ42 and Aβ43

We consider Aβ43 particularly informative when it is evaluated alongside matched Aβ40 and Aβ42 preparations.

Such comparisons allow peptide length to remain the principal experimental variable while other factors—purity, concentration, solvent history and incubation conditions—are controlled.

Handling and Aggregation

Like other long Aβ peptides, Aβ43 can be sensitive to preparation history. Reconstitution solvent, pH, ionic strength, temperature and incubation time can all change the initial aggregation state.

Researchers requiring additional Aβ lengths or sequence variants can use Custom Peptide Synthesis.

Frequently Asked Questions

What is the difference between Aβ42 and Aβ43?

Aβ43 contains one additional C-terminal threonine (Thr43) relative to Aβ42. Although this is only a one-residue difference, C-terminal length can substantially influence hydrophobicity, aggregation behavior, γ-secretase processing, and molecular recognition.

Where does Aβ43 occur in γ-secretase processing?

Aβ43 is an intermediate in a major processive cleavage pathway:

Aβ49 → Aβ46 → Aβ43 → Aβ40

It is therefore particularly useful for studies of γ-secretase processivity and C-terminal trimming.

Why study Aβ43 instead of only Aβ40 and Aβ42?

Comparing Aβ40, Aβ42, and Aβ43 allows researchers to examine how incremental changes in C-terminal length affect self-assembly and biological behavior. Aβ43 also provides information about γ-secretase processing that cannot be obtained from Aβ40 or Aβ42 alone.

Is Aβ43 aggregation behavior identical to Aβ42?

No. Aβ43 and Aβ42 can display different aggregation kinetics and structural behavior, but the magnitude and direction of those differences depend on experimental conditions. Buffer composition, concentration, and starting aggregation state should therefore be controlled carefully.

Research Use Only.

Amyloid β-Protein (1–43) | Human Aβ43 Research Peptide

Catalog No: AS2608

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