This is an N-terminal fragment of betaamyloid. It consists of amino acid residues 1 to 9. Truncated betaamyloid peptide (10-40) still forms amyloid fibrils and shows fibril polymorphism.
[Arg6]-β-Amyloid (1-40), England mutation 是具有生物活性的肽,与多种家族性常染色体显性阿尔茨海默病相关。特别地,这种英国突变,即位于第6位的His被Arg所替换,已报告可提高寡聚体形成动力学,加速初级纤维的种子化过程。此类寡聚体对神经元培养细胞展现出较高毒性。
Peptide fragment corresponding to residues 1 - 40 of Nogo-66, the domain of the myelin protein Nogo that inhibits axonal outgrowth. Acts as a competitive antagonist at the Nogo-66 receptor (NgR); blocks Nogo-66- and CNS myelin-induced inhibition of axonal
This synthetic peptide consists of amino acids 22 to 40 of betaamyloid protein. This peptide sequence is often used in betaamyloid structure and aggregation studies.
β-Amyloid (1-16) is an amyloidogenic protein fragment with a sequence derived from β-amyloid. It exhibits the ability to bind to metal ions, indicating its involvement in metal-binding processes. β-Amyloid, a peptide, is responsible for the formation of amyloid plaques in the brains of individuals affected by Alzheimer's disease (AD).
β-Amyloid (29-40), a fragment of the Amyloid-β peptide, possesses physical and chemical properties similar to those of viral protein fusion peptides. The C-terminal fragments (29-40 42) of Alzheimer's betaamyloid peptide can induce the fusion of liposomes.
β-Amyloid (1-38), derived from mice and rats, is a chemical compound comprising 38 amino acids, specifically residues 1-38 of the Aβ peptide. Notably, it serves as the primary constituent of amyloid plaques associated with Alzheimer's disease.
β-Amyloid (1-14),mouse,rat is a 1 to 14 fragment of Amyloid-β peptide. β-Amyloid (1-14),mouse,rat is produced through the proteolytic processing of a transmembrane protein, amyloid precursor protein (APP), by β- and γ-secretases. β-Amyloid (1-14),mouse,rat accumulation in the brain is proposed to be an early toxic event in the pathogenesis of Alzheimer’s disease, which is the most common form of dementia associated with plaques and tangles in the brain[1]. [1]. Chen GF, et al. Amyloidbeta: structure, biology and structure-based therapeutic development. Acta Pharmacol Sin. 2017 Sep;38(9):1205-1235.