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[Gly22]-Amyloid β-Protein (1–42) is the E22G Arctic variant of human Aβ42.
The peptide contains a glutamate-to-glycine substitution at residue 22 while retaining the strongly hydrophobic Ile41-Ala42 C-terminal extension characteristic of Aβ42.
Product Information
| Property | Specification |
|---|---|
| Product Name | [Gly22]-Amyloid β-Protein (1–42) |
| Mutation | E22G / Arctic |
| Sequence | DAEFRHDSGYEVHHQKLVFFAGDVGSNKGAIIGLMVGGVVIA |
| Length | 42 amino acids |
| Molecular Formula | C200H307N55O58S |
| Theoretical MW | ~4442.04 Da |
| Parent Peptide | Human Aβ42 |
| Peptide Type | Disease-associated Aβ42 variant |
| Research Areas | Oligomers, fibrils, familial AD, mutation-dependent amyloid assembly |
E22G Within the Aβ42 Background
The E22G substitution removes a negatively charged side chain from the central region of Aβ while the Aβ42 C-terminus maintains a strong tendency toward self-association.
This combination makes E22G Aβ42 useful for investigating how a defined disease-associated mutation changes the kinetics, intermediates and structural outcome of amyloid assembly.
E22G Aβ40 and E22G Aβ42 Are Different Experimental Materials
Both peptides contain the Arctic mutation, but they should not be reported simply as “Arctic Aβ.”
The additional Ile41 and Ala42 residues in the Aβ42 variant introduce a significant difference in hydrophobicity and aggregation behavior.
We recommend recording the complete identity as E22G Aβ40 or E22G Aβ42 in experimental records and procurement documents.
For direct wild-type versus mutant experiments, purity, preparation protocol, concentration and storage history should be matched wherever possible.
Additional analytical information is available through Peptide Quality Control.
Frequently Asked Questions
What is the Arctic E22G Aβ42 peptide?
It is a human Aβ42 variant in which glutamate at position 22 is replaced by glycine. The mutation is commonly referred to as E22G or the Arctic mutation.
Why is E22G Aβ42 useful in aggregation research?
The peptide combines a charge-altering mutation in the central region of Aβ with the strongly aggregation-prone Aβ42 C-terminus. It can therefore be used to investigate mutation-dependent oligomerization, protofibril formation, fibril structure, and assembly pathways.
What should be used as the control for E22G Aβ42?
Wild-type human Aβ42 is normally the most direct comparator because peptide length is identical and the E22G substitution remains the primary sequence variable.
Can E22G Aβ40 replace E22G Aβ42 in an experiment?
No. Although both contain the Arctic mutation, the two-residue C-terminal difference between Aβ40 and Aβ42 can significantly affect aggregation and molecular interactions. The exact peptide length should always be reported.
Research Use Only.