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Amyloid β-Protein (42–1) is the reverse-sequence analog of human Aβ1–42. It contains the same amino-acid composition and theoretical molecular mass as native Aβ42, but the residue order is reversed.
This design makes Aβ42–1 useful when researchers need to distinguish effects that depend on the native Aβ primary sequence from those associated with peptide composition, hydrophobicity, concentration, or nonspecific membrane interactions.
Product Information
| Property | Specification |
|---|---|
| Product Name | Amyloid β-Protein (42–1) |
| Sequence | AIVVGGVMLGIIAGKNSGVDEAFFVLKQHHVEYGSDHRFEAD |
| Length | 42 amino acids |
| Molecular Formula | C203H311N55O60S |
| Theoretical MW | ~4514.11 Da |
| Peptide Type | Reverse-sequence Aβ42 analog |
| Primary Comparator | Amyloid β-Protein (1–42), Human |
| Research Areas | Sequence controls, aggregation, membrane interaction, cellular response |
Reverse Aβ42 as an Experimental Control
Reverse Aβ42 is frequently used as a control peptide, but it should not automatically be considered chemically or biologically inert.
The sequence remains 42 residues long and retains the same overall amino-acid composition as native Aβ42. Under some conditions it may still self-associate or interact with membranes.
Its most appropriate role is therefore as a sequence-orientation comparator.
Reverse Sequence vs Mirror-Image Aβ42
Aβ42–1 and ent-Aβ42 answer different experimental questions.
Reverse Aβ42 changes the order of the residues while retaining normal L-amino-acid stereochemistry. An all-D Aβ42 peptide retains sequence order but changes molecular chirality.
For studies focused specifically on native sequence recognition, Aβ42–1 may be the more informative control.
Experimental Considerations
For direct Aβ1–42 versus Aβ42–1 comparisons, We recommend matching peptide concentration, purity, terminal chemistry, reconstitution method, buffer, and incubation time.
Aggregation-prone peptides can produce substantially different results if their initial physical states are not controlled.
Application-dependent purity considerations are available through Recommended Peptide Purity.
Frequently Asked Questions
What is Amyloid β-Protein (42–1)?
Amyloid β-Protein (42–1) is the reverse-sequence analog of Aβ1–42. It contains the same amino-acid composition as native Aβ42 but places the residues in the opposite order.
Is reverse Aβ42 a negative control?
It is frequently used as a sequence control, but calling it universally “inactive” is too strong. Reverse Aβ42 remains a relatively long and hydrophobic peptide and can still display self-association or membrane interactions under some experimental conditions.
What question does reverse Aβ42 help answer?
It helps determine whether an observed response depends specifically on the native Aβ42 primary sequence rather than simply on peptide concentration, amino-acid composition, hydrophobicity, or nonspecific exposure to a 42-residue peptide.
Should Aβ42 and Aβ42–1 be prepared using the same protocol?
Yes. For comparative studies, concentration, purity, terminal state, solvent history, buffer, incubation temperature, and incubation time should be matched as closely as possible. Different preparation histories can produce different aggregation states and complicate interpretation.
Research Use Only.