[Gln22]-Amyloid β-Protein (1–40) is the E22Q Dutch variant of human Aβ40, in which the native glutamate at residue 22 is replaced by glutamine.

This charge-neutralizing substitution is associated with hereditary cerebral hemorrhage with amyloidosis–Dutch type and has become an important research model for cerebral amyloid angiopathy (CAA), vascular amyloid deposition, fibril formation and mutation-dependent Aβ assembly. Unlike many Aβ variants studied primarily in the context of parenchymal plaques, the Dutch mutation has a particularly strong association with cerebrovascular amyloid pathology.

Product Information

The E22Q sequence, molecular formula and molecular mass are consistent with independently cataloged [Gln22]-Aβ1–40 reference material.

The Dutch E22Q Mutation

Residue 22 lies within a central region of Aβ involved in intermolecular organization and fibril assembly.

Replacing glutamate with glutamine removes a negatively charged side chain while preserving a polar amide-containing residue. This apparently small change can substantially influence Aβ40 aggregation, fibril structure, clearance and interaction with cerebrovascular cells.

Studies comparing wild-type and Dutch Aβ40 have shown enhanced fibril formation and pronounced vascular-associated pathological behavior for the E22Q sequence.

AβDutch and Cerebral Amyloid Angiopathy

The Dutch mutation is particularly relevant to research involving cerebral amyloid angiopathy rather than simply general amyloid plaque formation.

Human and experimental studies indicate that E22Q Aβ has a strong tendency toward vascular deposition. In transgenic models expressing AβDutch, vascular amyloid and hemorrhagic pathology increased while parenchymal deposition was comparatively reduced.

This makes [Gln22]-Aβ40 useful for laboratories investigating the mechanisms that determine whether amyloid accumulates in cerebral blood vessels versus brain parenchyma.

Research Applications

[Gln22]-Aβ40 can support studies of mutation-dependent fibrillation, amyloid aggregation kinetics, cerebral vascular deposition, cerebrovascular smooth-muscle responses, amyloid–protein interactions and comparative studies of hereditary CAA variants.

It is also useful when comparing different residue-22 mutations such as:

E22Q Dutch Aβ40

E22G Arctic Aβ40

These peptides modify the same native glutamate residue but produce chemically and biologically distinct sequence variants.

We recommend identifying the exact substitution in experimental records rather than referring generically to a “position-22 Aβ mutant.”

Selecting the Correct Comparator

For experiments focused specifically on the Dutch mutation, wild-type human Aβ40 is the most appropriate primary comparator.

Using E22G Aβ40 or Aβ42 as the only control would introduce additional variables involving residue chemistry or peptide length.

Wild-type and mutant materials should ideally be matched for purity, terminal state, reconstitution method, concentration and incubation conditions.

Aggregation and Sample Preparation

Like other Aβ40 variants, [Gln22]-Aβ40 can be highly sensitive to sample history.

Aggregation kinetics may be influenced by initial monomerization, solvent, ionic strength, concentration, temperature and incubation time. These variables should therefore be controlled when comparing E22Q with wild-type or other CAA-associated sequences.

We think this is particularly important for mutation-comparison experiments, where an uncontrolled difference in initial aggregation state can obscure the actual effect of the amino-acid substitution.

Additional batch-specific analytical information can be supported through Peptide Quality Control.

Researchers requiring additional CAA-associated mutations, labeled Aβ variants or custom sequence combinations can use Custom Peptide Synthesis.

Frequently Asked Questions

What mutation does [Gln22]-Amyloid β-Protein (1–40) contain?

It contains the E22Q mutation, replacing glutamate at residue 22 with glutamine.

What is the Dutch amyloid mutation?

The Dutch mutation is the E22Q substitution in Aβ, associated with hereditary cerebral hemorrhage with amyloidosis–Dutch type and severe cerebral amyloid angiopathy.

What is the sequence of E22Q Aβ40?

The sequence is:

DAEFRHDSGYEVHHQKLVFFAQDVGSNKGAIIGLMVGGVV

Is Dutch Aβ40 the same as Arctic Aβ40?

No. Dutch Aβ40 contains E22Q, whereas Arctic Aβ40 contains E22G. Both affect residue 22 but represent different molecular variants and should not be used interchangeably.

Research Use Only.