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Alzheimer’s disease-associated Aβ42 peptide

 

Aggregation of the amyloid-beta peptide (A?) in the brain is strongly associated with Alzheimer┬┤s disease (AD). This process is highly heterogeneous and transient in nature, thus hindering identification of the exact molecular form of A? responsible for the neurotoxicity observed in this disease. Therefore, characterizing A? aggregation is of utmost importance to make headway in the field of AD. Nuclear magnetic resonance spectroscopy (NMR), a technique used to obtain structural information, holds great potential to achieve this goal, as it could contribute to determining the structure of A? aggregate forms. However, it requires large amounts of peptide, as well as isotopic labels that are introduced through the A? peptide production process.

In this article, we report a new and straightforward production protocol to obtain the A? most strongly linked to AD, the so-called A?42 form, with the required labels for NMR experiments. Specifically, we describe an inexpensive strategy through which to obtain [U-15N]- and [U-2H,13C,15N]-labeled A?42. Notably, this approach does not require reversed phase high performance liquid chromatography (RP-HPLC), a costly and time-consuming purification technique widely used in previously reported A? production protocols. Instead, all the purification steps required in our production protocol can be performed with the fast protein liquid chromatography system (FPLC), which is widely available. The peptides that we obtained are of high purity and have the required isotope labeling to support NMR-based structural studies.Therefore, we conclude that this strategy offers a simpler and inexpensive approach to obtain isotopically labeled A?42 than previously described methods, thereby paving the way for NMR-based A? structural studies.

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For more information, please visit: http://www.eurekaselect.com/149791/article

 

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