amyloid β-peptide

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].

Biotin-amyloid-β (1-42) peptide is an affinity probe that allows amyloid-β (1-42) (Aβ42) to be detected or immobilized through interaction with the biotin ligand. It has been used to identify Aβ42 interaction partners in rat hippocampal synaptosomal membranes.

Amyloid-β (1-42) (Aβ42) is a neurotoxic 42-amino acid protein fragment found in amyloid plaques in postmortem cerebral cortex from patients with Alzheimer's disease.1,2,3Aggregation of Aβ42 results in the formation of neurotoxic fibrils or globular oligomers.1Aβ42 accumulates in the brain of many transgenic mouse models of Alzheimer's disease and, in many models, the onset of amyloid deposition positively correlates with deficits in spatial learning and memory.4 1.Wolfe, M.S.Therapeutic strategies for Alzheimer's diseaseNat. Rev. Drug Discov.1(11)859-866(2002) 2.Iwatsubo, T., Odaka, A., Suzuki, N., et al.Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)Neuron13(1)45-53(1994) 3.Hardy, J.A., and Higgins, G.A.Alzheimer's disease: The amyloid cascade hypothesisScience256(5054)184-185(1992) 4.Jankowsky, J.L., and Zheng, H.Practical considerations for choosing a mouse model of Alzheimer's diseaseMol. Neurodegener.12(1)89(2017)

Amyloid-β (1-8) is a wild-type control for the mutation-containing amyloid-β (1-8, A2V) peptide .

Amyloid-β (1-8, A2V) is a truncated form of amyloid-β (Aβ) that contains a valine to alanine substitution at position 2 of the Aβ numbering convention (Aβ A2V), which corresponds to position 673 of the amyloid precursor protein (APP) numbering convention (APP A673V). An Aβ (1-40) (Aβ40) A2V peptide increases the production of Aβ and the rate and amount of amyloid fibril formation in vitro, effects that can be reduced by coincubation with wild-type Aβ40. Aβ40 and Aβ42 levels are increased in CHO cells expressing the Aβ A2V mutation and in fibroblasts derived from patients with the Aβ A2V mutation. As a homozygous mutation, Aβ A2V is correlated with Alzheimer's disease with distinctive pathological features, but disease does not develop in patients with a heterozygous Aβ A2V mutation.

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.

TAMRA-Amyloid-β (1-42) peptide is a fluorescently labeled peptide. Amyloid-β (1-42) (Aβ42) is a neurotoxic 42-residue protein fragment found in amyloid plaques in postmortem cerebral cortex from patients with Alzheimer's disease. Aggregation of Aβ42 results in the formation of neurotoxic fibrils or globular oligomers. TAMRA-Amyloid-β (1-42) peptide is a labeled form of Aβ42 containing carboxytetramethyl rhodamine (TAMRA), which displays excitation/emission maxima of 543/572 nm, respectively.

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.

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.

Citrullinated amyloid-β(1-40) peptide (human) (Citrullinated Aβ (1-40)) is a modified form of β-Amyloid (1-40) that has undergone citrullination at the Arg5 position. Compared to the unmodified β-Amyloid (1-40), it exhibits increased transient formation of soluble oligomers and insoluble aggregates composed of twisted parallel β-sheets.

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

Rutin (Quercetin 3-O-rutinoside), a flavonoid, has a variety of biological activities including antiallergic, anti-inflammatory, antiproliferative, and anticarcinogenic properties.

DAPT (LY-374973) is a γ-secretase inhibitor that inhibits total Aβ and Aβ42 (IC50=115/200 nM) and is orally active. DAPT is also a Notch inhibitor. DAPT induces cell differentiation, autophagy and apoptosis.

Colivelin is a neuroprotective peptide and activator of STAT3. Colivelin is a hybrid peptide synthesized to enhance the neuroprotective effects of humanin (HN).

Rutin hydrate (Sophorin), a kind of glycoside, widely exists in many plants including citrus fruit.

Tramiprosate (Alzhemed) is an orally active, blood-brain-barrier-crossing, naturally occurring amino acid found in a variety of red seaweeds that binds soluble Aβ and maintains it in a non-protofibrillar form.It is a GABA analog with neuroprotective, anticonvulsant, and antihypertensive activity.

Hematoxylin (Natural Black 1) is a dye obtained from the heartwood of logwood (Haematoxylon campechianum Linn., Leguminosae) used as a stain in microscopy and in the manufacture of ink.

Geniposide is an iridoid glycoside with a variety of biological activities including neuroprotective, anti-diabetic, antiproliferative, and antioxidative activity. Geniposide has been shown to regulate Nrf2 translocation.

Ginsenoside Rg1 (Panaxoside Rg1) is a class of steroid glycosides, and triterpene saponins found exclusively in the plant genus Panax (ginseng). It improves spatial learning and increase hippocampal synaptophysin level in mice, plus demonstrates estrogen-like activity.

Notoginsenoside R1 (Sanchinoside R1) has been shown to exhibit antioxidant, antiapoptotic, anti-inflammatory, and immune-stimulatory properties.

Methyl tridecanoate is a natural product.

Qingyangshengenin B (Otophylloside B) is a C-21 steroidal glycoside isolated from Qingyangshen. Qingyangshengenin B protects against Aβ toxicity, which decreases Aβ deposition by decreasing the expression of Aβ at the mRNA level. Qingyangshengenin B has antiepileptic and anti-aging effects, it can extend lifespan, increase heat stress-resistance, delay body paralysis, and increase the chemotaxis response in C. elegans models of Alzheimer's disease. Otophylloside B can suppress the seizure-like locomotor activity caused by pentylenetetrazole in zebrafish.

JLK6 was a gamma-secretase inhibitor that does not interfere with Notch signalling

Aftin-4, an amyloid forty-two inducer, activates γ-secretase, promoting the generation of amyloid-β-1-42 (Aβ1-42) from amyloid-β protein precursor. Aftin-4(Aftin4) increased Aβ-1-42, but not Aβ-1-40 in mouse hipppocampus, accompanied by learning deficits and mitochondrial ultrastructural changes similar to those found in the brains of patients with AD. Aftin-4(Aftin4) can thus be used to induce a rapid, acute Alzheimer's disease-like toxicity in the rodent brain.