Amyloid Beta Peptide Explained
The Amyloid Beta Peptide, sometimes called AB42, is found in the brains of individuals having Alzheimer’s or Down’s Syndrome. As you might know, a peptide consists of two or more amino acids that are linked together, with the carboxyl group of each amino acid connected to the amino group of the next with a type -OC-NH- bond. The Amyloid Beta Peptide is 39 to 43 amino acids long from the membrane protein, located in the brains of people with Alzheimer’s. Many scientists believe that the Amyloid Beta Peptide is responsible for causing Alzheimer’s disease. Alzheimer’s patients have Amyloid Plaques, deposits of extracellular matter, in their brains that are primarily made up of Amyloid Beta Peptides. Similar plaques are also found in patients with Lewy Body Dementia and muscle diseases. It is believed that Amyloid Beta Peptides may be responsible for the production of components that layer cerebral blood vessels in congophilic angiopathy.
Biologically, Amyloid Beta Peptide can be described as 42-Residue amyloid ß-protein fragment. The most common form of the peptide in Down’s Syndrome and Alzheimer’s patients is neurotoxic. It has a purity of >95%.
Amyloid Beta Peptides Research Considerations
When using Amyloid Beta Peptides for research purposes, you can measure them in multiple ways. One such measurement allows location determination through immunostaining, semi-quantitatively. Another method of measuring Amyloid Beta Peptides allows measurement of the earliest stages of inhibition and aggregation, is optical and called dual polarization interferometry. The process can be observed on lipid bilayer constructs.
When preparing Amyloid Beta Peptides solutions they should be used in the same day. If you must prepare them in advance for research, store them in tightly sealed vials at -20°C. You can use them up to one week after preparing the solution. When you open your Amyloid Beta Peptides solution, allow it to sit for at least 1 hour at room temperature prior to use.
Amyloid Beta Peptides Cannot Be Crystallized
Amyloid Beta Peptides cannot be crystallized as they do not gain a unique tertiary fold in solution. The majority of structural data is derived from molecular dynamics and nuclear magnetic resonance (NMR). The probable ways that amyloid beta peptides can destroy and inflict neuronal death include reactive oxygen species generation throughout its self-aggregation process. When the neuron membranes are in utero and this happens, lipid peroxidation occurs as well as the production of 4-hydroxynonenal, which is a toxic aldehyde. This aldehyde harms the mechanisms of ion-motive ATPases, glutamate transporters and glucose transporters. In turn, amyloid beta peptides foster mitochondrial impairment, synaptic membrane depolarization and an excess of calcium influx. Amyloid beta peptide aggregations upset the membranes while in utero.