amyloid-beta peptide

Amyloid β Peptide (42-1)(human) acetate is the inactive form of Amyloid β Peptide (1-42). Amyloid β Peptide (42-1)(human) acetate is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.

GSNKGAIIGLM(131602-53-4(free base)) (Amyloid beta-peptide(25-35)) is the fragment Aβ(25-35) of the Alzheimer's amyloid β-peptide.

Beta-Sheet Breaker Peptide iAβ5 Acetate (C33H43N5O8) inhibit amyloidogenesis in rat brain models.

Beta-Amyloid(1-14),mouse,rat is a 1 to 14 fragment of Amyloid-β peptide. This peptide is amino acids 1 to 14 fragment of Beta-Amyloid peptide.

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

Amyloid beta-protein(1-40) Arctic variant (Ab40ARC (E22G)), featuring a glycine at position 22 (Gly22), is a peptide utilized in Alzheimer's disease research [1].

β-Amyloid (25-35) (Aβ25-35) is the fragment Aβ(25-35) of the Alzheimer's amyloid β-peptide. Which has shown neurotoxic activities in cultured cells.

[Asn23]-beta-Amyloid (1-42), Iowa mutation, is a biologically active peptide with increased aggregation propensity and fibril toxicity. This mutation involves the substitution of Aspartic acid (Asp) at position 23 with Asparagine (Asn), contributing to autosomal dominant Alzheimer's Disease and associated with severe cerebral amyloid beta-protein angiopathy (CAA) due to a missense alteration at position 694 of the amyloid precursor protein (APP) gene.

β-Amyloid peptide(16-20), with the amino acid sequence (KLVFF) derived from Amyloid-β (Abeta), functions as an efficient inhibitor of Abeta fibril formation. This compound is modified with RG-/-GR-NH2 residues at both its N- and C-terminal ends to enhance solubility [1].

Amyloid-Forming peptide GNNQQNY, a biologically active heptapeptide derived from the N-terminal prion-determining domain of yeast Sup35, is instrumental in amyloid fibril formation. Its atomic oligomeric structure has been detailed, serving as an excellent model for investigating early-stage aggregation. The peptide can form three stable β-sheet structures: in-register parallel, off-register parallel, and anti-parallel. Notably, the in-register parallel dimer aligns closely with amyloid β-sheet architecture, relying on fewer interpeptide hydrogen bonds and emphasizing hydrophobic interactions, which enhances conformational entropy relative to the anti-parallel arrangement.

β-Amyloid 15-21 acetate (Beta-Amyloid (15-21) acetate) 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 (1-42), human, is a 42-amino acid peptide integral to the pathogenesis of Alzheimer disease.

β-Amyloid (31-35) (β-Amyloid 31-35) is the shortest sequence of native Amyloid-β peptide.

(Pyr11)-Amyloid β-Protein (11-40) (Aβ11pE-40), a peptide, is utilized in Alzheimer's disease research [1].

[Arg6]-β-Amyloid (1-42), England mutation, is a biologically active peptide linked to autosomal dominant Alzheimer's Disease in various kindreds. The English (H6R) mutation disrupts H6 interactions due to alterations in the beta-amyloid precursor gene.

Rat form of the beta-Amyloid (1-40) peptide

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. Beta amyloid (22-35) is a synthetic truncated fragment of beta-amyloid peptide.

β-Amyloid (29-40) is a fragment of Amyloid-β peptide. Alzheimer's beta amyloid peptide (29-40 42) C-terminal fragments exhibit physical and chemical properties similar to fusion peptides of viral proteins, inducing liposome fusion in vitro.

β-Amyloid (1-16) rat is a fragment of the amyloid beta (Abeta) peptide's metal-binding domain, containing three amino acid substitutions compared to its human counterpart, which confer reduced susceptibility to Alzheimer's disease-like neurodegeneration in rats and mice [1].

β-Amyloid (1-40), England mutation, is a biologically active peptide with a histidine (His) to arginine (Arg) substitution at position 6, known to enhance oligomerization kinetics that serve as fibril seeds and increase neurotoxicity in cultured neurons. This alteration is one of several mutations in the beta-amyloid precursor gene implicated in autosomal dominant Alzheimer's Disease across multiple kindreds.

β-Amyloid (1-14), mouse, rat, is a 1-14 fragment of the Amyloid-β peptide.

This synthetic peptide consists of amino acids 1 to 17 of beta amyloid protein. This peptide can be employed in beta amyloid solubility studies.

β-Amyloid (33-40) is a peptide composed of amino acids 33 to 40 from the beta-amyloid protein.

β-Amyloid (35-42), a peptide derived from the beta-amyloid protein, encompasses amino acids 35 through 42.

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. β-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 disease, affecting approximately 10% of the population over 60.

This synthetic peptide consists of amino acids 1 to 20 of beta amyloid protein.

This is an N-terminal fragment of beta amyloid. It consists of amino acid residues 1 to 9. Truncated beta amyloid peptide (10-40) still forms amyloid fibrils and shows fibril polymorphism.

This synthetic peptide consists of amino acids 22 to 40 of beta amyloid protein. This peptide sequence is often used in beta amyloid structure and aggregation studies.

neuroprotective peptide that binds to amyloid beta (Aβ)

This is a fragment of beta-amyloid peptide. It has amino acids 1 through 34.

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 beta amyloid protein. It is utilized to study the kinetics of beta amyloid formation.

'(Asp37)-Amyloid β-Protein (1-42) [1]' refers to the G37D mutant variant of the wild-type Amyloid-beta (1-42) peptide.

β-Amyloid (42-1), human, is the inactive form of Amyloid β Peptide (1-42), which plays a pivotal role in the pathogenesis of Alzheimer's disease.

β-Amyloid (1-42), (rat mouse) (TFA), is a 42-amino acid peptide fragment employed in the study of Alzheimer's disease.

[Asn23] β-Amyloid (1-40), Iowa mutation, is a biologically active peptide linked to autosomal dominant Alzheimer's Disease in multiple families. This involves the substitution of Asp 23 with Asn, causing severe cerebral amyloid beta-protein angiopathy (CAA). Individuals with this mutation exhibit a missense alteration in the APP gene at position 694, resulting in the mutated β-amyloid peptide aggregating more quickly and forming toxic fibrils.