tamra-amyloid-b peptide

Small Cardioactive Peptide B SCPB acetate (Small Cardioactive Peptide B SCPB acetate (84746-43-0 free base)) is a neurally active peptide, stimulates adenylate cyclase activity in particulate fractions of both heart and gill tissues with EC50s of 0.1 and 1.0 μM, respectively.

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.

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-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.

SP-B peptide is an antimicrobial agent with demonstrated antifungal activity against Cryptococcus neoformans, Candida albicans, and Aspergillus fumigatus strains[1].

Thioether-cyclized helix B peptide (CHBP) enhances metabolic stability and exerts renoprotective effects by promoting autophagy through the inhibition of mTOR C1 and activation of mTOR C2 [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.

Peptide B, Bovine, an immunoregulatory peptide derived from αs1-casein B-8P (f1-13) in bovine milk, is predominantly generated during maturation and exhibits antihypertensive effects [1] [2].

Small Cardioactive Peptide B (SCPB), a neurally active peptide, stimulates adenylate cyclase activity in particulate fractions of both heart and gill tissues with EC50s of 0.1 and 1.0 μM, respectively.

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

Thioether-cyclized helix B peptide, CHBP (TFA), is the trifluoroacetic (TFA) salt of CHBP, enhancing metabolic stability and exhibiting renoprotective effects by promoting autophagy through inhibition of mTOR C1 and activation of mTOR C2 [1].