β amyloid (18 28)

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.

β-Amyloid(17-28) human is a fragment of the β-amyloid peptide (Abeta) associated with Alzheimer's disease (AD), promoting the aggregation of the full-length β-Amyloid40 into toxic aggregates [1]. This lipid-induced amyloid core segment is implicated in AD pathogenesis.

β-Amyloid(28-35) human is a neurotoxic β-amyloid peptide fragment that contributes to Alzheimer's disease pathogenesis by interacting with neuronal membranes, modulating its secondary structure and toxicity. It also exhibits anisotropic effects on the acidic phospholipid DPH, thereby increasing the internal fluidity within lipid membrane bilayers [1].

β-Amyloid (1-28) is a β-Amyloid protein fragment involved in metal binding.

β-Amyloid (12-28) (TFA), a peptide fragment of the β-amyloid protein (β1-42)—a 42 amino acid protein primarily found in senile plaque cores—exhibits aggregation properties. This compound holds significance for research into Alzheimer’s disease, highlighting its potential utility in understanding the disease's pathology [1].

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.

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.