Amyloid β-Protein (42-1) is an unusual variant of the amyloid β (Aβ) peptide featuring a reversed amino acid sequence, with residues numbered from the C-terminal (position 42) to the N-terminal (position 1) of the native Aβ(1-42) sequence. This synthetic reverse peptide disrupts the natural structural conformation and hydrophobic interactions critical for Aβ aggregation, serving as a negative control in studies to investigate the role of primary sequence directionality in fibril formation, neurotoxicity, and receptor binding. Unlike the native Aβ(1-42), which readily forms toxic oligomers and plaques associated with Alzheimer’s disease, the reversed sequence (42-1) typically exhibits reduced aggregation propensity and altered biological activity. In research, it is used to validate the specificity of Aβ-mediated interactions, explore structural requirements for pathological assembly, and assess the impact of sequence orientation on biophysical properties. While not naturally occurring, this variant highlights the importance of amino acid order in Aβ’s pathogenicity, supporting mechanistic studies of amyloidosis and the development of sequence-specific therapeutic strategies.

Chemical Formula: C203H311N55O60S

Molecular Weight: 4514.14

Sequence: Ala-Ile-Val-Val-Gly-Gly-Val-Met-Leu-Gly-Ile-Ile-Ala-Gly-Lys-Asn-Ser-Gly-Val-Asp-Glu-Ala-Phe-Phe-Val-Leu-Lys-Gln-His-His-Val-Glu-Tyr-Gly-Ser-Asp-His-Arg-Phe-Glu-Ala-Asp

Purity: From crude to 98%

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