Amyloid β (Aβ) are peptides of 36–43 amino acids that are derived from the amyloid precursor protein (APP) by cleavage with β- and γ- secretase. Aβ are the main components of amyloid plaques and therefore crucially involved in Alzheimer’s disease. The biological function of Aβ is still unexplained, but they are claimed to be neurotoxic as they form extracellular deposits in the brain and so can harm the cellular membrane.
To understand the function of the Aβ and for the research of Alzheimer’s disease, it is important to develop a reliable analysis for Aβ.
However, this is not trivial as the Aβ peptides such as Aβ (1–42) are highly hydrophobic which leads to the formation of aggregates.
A method for the simultaneous determination of four Amyloid β using YMC-Triart Bio C4 has been developed by YMC. As the hydrophobic Aβ have the tendency to form aggregates a stationary phase with lower hydrophobicity and larger pore is needed, therefore YMC-Triart Bio C4 was chosen. Due to the high chemical stability of YMC-Triart Bio C4 it is possible to do rapid method optimisation for complex mixtures of peptides and proteins utilising the wide pH and temperature range available. YMC-Triart Bio C4 is available with 3 and 5 μm for HPLC, as well as with fully scalable 1.9 μm for UHPLC.
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