Alzheimer's disease is the most common form of brain disorder amongst  the elderly. In 2006 alone, about 26.6 million people worldwide were  affected by this disease and it is predicted to increase by 1 in every  85 people by year 2050. Alzheimer's disease is believed to be caused by  the accumulation of amyloid peptides, which are generated by cleavage of  the amyloid precursor protein by beta secretase (BACE1) followed by  gamma secretase. Since BACE1 cleavage is limiting for the production of  amyloid beta,1 an approach for the treatment of this disease   is to generate inhibitors targeting BACE1. BACE2, a homologue of BACE1  is reported to function as an alternate alpha-secretase2 and  thereby prevent the formation of amyloid plaques. Several inhibitors for  BACE1 are reported, however their selectivity over BACE2 has not been  addressed so far. In order to design selective inhibitors for BACE1,  complete structural insight of both enzymes is required. We present a  structural study on the isozymes, first of its kind, using MD  simulations, which might enable the design of more selective inhibitors.1 Stockley JH, O'Neill C., Cell. Mol. Life. Sci. 2008  , 65(20):3265-89.2 Yan R, Munzner JB, Shuck ME, Bienkowski MJ., J. Biol. Chem. 2001,   276(36):34019-27.

Insights into the structural features of BACE: Comparison of the isozymes

243rd National Meeting (2012)

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