Amyloid-beta peptide (N-terminal region) (Aβ (N-terminus))

The N-terminal amyloid-beta region comprises the initial segment of the Aβ peptide, typically residues 1–16 or 1–28, derived from proteolytic cleavage of amyloid precursor protein (APP). Structural research highlights its involvement in intermolecular interactions during fibrillation and its importance for pathogenic aggregation. Modifications and mutations in the N-terminal can alter aggregation kinetics, fibril stability, and neurotoxicity, influencing Alzheimer's disease risk and progression. It is biologically and therapeutically relevant as the binding site for several antibodies and as a determinant of amyloid structure and toxicity. N-terminal modifications (e.g., phosphorylation, truncation) yield amyloid species with distinct pathological properties.

Other names

N-terminal AβAβ (1–16), Aβ (1–28), Aβ (N-terminal segment)N-terminal amyloid-beta peptide

Immunotherapy: monoclonal antibodies can bind the N-terminal region of Aβ, promoting clearance or neutralizing toxicity. Inhibition of aggregation: small molecules or peptides can bind the N-terminus to prevent β-sheet formation and toxic aggregate evolution. Modulation of proteolytic processing: altering secretase activity to affect Aβ N-terminus generation.