SDD-AGE

In biochemistry and molecular biology, SDD-AGE is short for Semi-Denaturating Detergent Agarose Gel Electrophoresis.

This method is very useful for studying prions and amyloids, which are characterized by the formation of proteinaceous polymers.

Use of this method allowed researchers to understand that at least some types of prion aggregates existed in a two-level structure - protein molecules grouped into polymers, which are very stable and withstand treatment with 2% SDS at room temperature, and aggregates, which are bundles of polymers, that dissociate under these conditions.

The method was created in the Molecular Genetics laboratory of the Russian Cardiology Research Institute and was published in 2003 by Kryndushkin et al.[1] The original method used a TAE buffering system and incorporated a modified vacuum blotting system for the transfer of proteins onto a membrane (originally PVDF).

[8] DD-AGE, a further variation of the method that uses fully denaturing conditions - including reducing agents such as dithiothreitol (DTT) and heat denaturation at 95°C - is suitable for the analysis of heat-stable inclusion bodies of polyglutamine proteins.