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ent-Amyloid β-Protein (1–42), also referred to as D-Aβ42, is the mirror-image enantiomer of naturally occurring L-Aβ42. The primary sequence is retained, while the chiral amino-acid residues are present in their D-configuration.
This design provides a useful experimental tool for distinguishing intrinsic peptide self-assembly from biological interactions that depend on stereochemical recognition.
Product Information
| Property | Specification |
|---|---|
| Product Name | ent-Amyloid β-Protein (1–42) |
| Sequence Order | DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA |
| Configuration | All chiral residues in D-configuration |
| Length | 42 amino acids |
| Molecular Formula | C203H311N55O60S |
| Theoretical MW | ~4514.11 Da |
| Peptide Type | Mirror-image Aβ42 enantiomer |
| Research Focus | Chirality, proteolysis, stereospecific recognition, amyloid assembly |
| Purity | From crude to 98% |
What Does an All-D Aβ42 Test?
D-Aβ42 is different from a scrambled peptide or reverse-sequence control.
It preserves sequence order and chemical composition while reversing molecular chirality. It can therefore help distinguish interactions that require stereochemical recognition by receptors, enzymes, antibodies or other biomolecules from effects caused largely by physicochemical properties.
D-Aβ42 should not automatically be described as a non-aggregating peptide. Mirror-image Aβ can still self-associate, while its interaction with chiral biological systems may differ substantially from the natural L-form.
Experimental Comparison
For D-versus-L studies, We recommend matching concentration, purity, terminal chemistry, buffer and aggregation protocol.
The different proteolytic stability of D-amino-acid peptides can become particularly important during long incubations in biological matrices.
Custom D-amino-acid amyloid sequences are available through Custom Peptide Synthesis.
Frequently Asked Questions
What does “ent-Amyloid β-Protein (1–42)” mean?
The prefix ent- indicates the mirror-image enantiomer of conventional Aβ42. The amino-acid sequence order is retained, but the chiral residues are present in their D-configuration rather than the natural L-configuration.
Is D-Aβ42 a non-aggregating control?
Not necessarily. D-Aβ42 can still undergo self-association and amyloid-like assembly. Its main experimental value is that it changes molecular chirality while retaining sequence order and composition, allowing researchers to investigate stereospecific biological recognition.
What is the difference between ent-Aβ42 and reverse Aβ42?
ent-Aβ42 retains the normal Aβ1–42 residue order but reverses amino-acid chirality. Reverse Aβ42 retains conventional L-amino acids but reverses the sequence from residues 42 to 1. These two peptides therefore test different experimental variables.
Why can D-Aβ42 be useful in proteolysis studies?
Many biological proteases are stereoselective and recognize natural L-amino-acid substrates more efficiently than their D-enantiomers. D-Aβ42 can therefore help distinguish protease-dependent effects from aggregation or other physicochemical effects.
Research Use Only.