The amyloid β-protein is a 39- to 43-amino acid polypeptide that is the primary constituent of senile plaques and cerebrovascular deposits in Alzheimer's disease and Down's syndrome. Additionally it acts as an inhibitor of the ubiquitin-dependent protein degradation in vitro.
Amyloid β-peptide fragment; minimum section required to bind to brain proteins. Binds with high affinity to α7-nicotinic ACh receptors, and impairs memory retention following central administration in mice in vivo.
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).
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.
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.
Intracerebroventricular administration of synthetic peptides Beta-amyloid (12-20), (12-28), and (18-28) causes amnesia in mice. These peptides have only amino acid residues VFF at position 18 to 20 in common, suggesting the amnestic effect of the triad.
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.
β-Amyloid (11-22) is a peptide fragment of β-Amyloid. Beta-amyloid peptide (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.
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.
Anionic interaction of Beta-amyloid (1-11) with Factor XII is suspected to cause massive activation of the C4 (complement 4) system in the cerebrospinal fluid of Alzheimer's disease patients.
β-amyloid (12-28) TFA, a peptide fragment of β-amyloid protein (β1-42), is the major component of senile plaque cores. β-amyloid (12-28) has aggregation properties and the potential for Alzheimer's disease research.
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-amyloid peptide.
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.