Amyloid-β (25-35) (Aβ (25-35)) is an 11-residue fragment of the Aβ protein that retains the physical and biological characteristics of the full length peptide. It forms fibrils that react to thioflavin T and Congo red and are organized in a cross-β arrangement of β-strands similar to Aβ (1-40) and Aβ (1-42) fibrils. Aggregated Aβ (25-35) decreases the viability of rat adrenal PC12 cells. It also decreases the viability of primary rat cortical neurons at concentrations ranging from 1 nM to 30 μM. In vivo, intracerebral injection of Aβ (25-35) (20 nmol) in rats induces lesions of neuronal and tissue loss. Aggregated Aβ (25-35) administered intracerebroventricularly to rats induces learning and memory impairments in the Y-maze, novel object recognition, and contextual fear conditioning tests.
Amyloid precursor c-terminal peptide has the amino acid sequence Gly-Tyr-Glu-Asn-Pro-Thr-Tyr-Lys-Phe-Phe-Glu-Gln-Met-Gln-Asn. APP is best known as the precursor molecule whose proteolysis generates beta-amyloid (Aβ), a 37 to 49 amino acid peptide whose am
[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。
Antibodies corresponding to beta-amyloid (4-10) are effective in vivo inhibitors of cytotoxicity, amyloid plaque formation and special memory disturbances in mice. This peptide does not elicit an inflammatory response.
β-Amyloid (22-35) is a 14-aa peptide, shows aggregates and induces neurotoxicity in the hippocampal cells. Betaamyloid (22-35) is a synthetic truncated fragment of beta-amyloidpeptide.
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 betaamyloidpeptide can induce the fusion of liposomes.
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.
β-amyloid (15-21) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease. This fragment is involved in beta sheet formation.
β-Amyloid (11-22) is a peptide fragment of β-Amyloid. Beta-amyloidpeptide (Abeta), the primary component of amyloid plaques in the brains of Alzheimer’s patients, is believed to be the cause of Alzheimer’s Disease (AD), the most common neurodegenerative disorder.
This is an N-terminal fragment of betaamyloid. It consists of amino acid residues 1 to 9. Truncated betaamyloidpeptide (10-40) still forms amyloid fibrils and shows fibril polymorphism.
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.
Amyloid (1-42), rat is a polypeptide composed of 42 amino acids. It is toxic to hippocampal slices and can be used in the study of alzheimer's disease.
β-Amyloid (13-27) is a synthetic peptide comprising amino acids 26 to 40 of the betaamyloid protein. It is utilized to study the kinetics of betaamyloid formation.