My collaborators, Dr. Wang's group, extended our initial studies and just published NMR results on Aβ-ABAD binding, which forms a direct link between Aβ and mitochondrial toxicity. This paper examined the thermodynamics as well as conformational and functional consequences of the Aβ-ABAD interaction. Surface plasma resonance showed that the binding between Aβ and ABAD is mainly driven by hydrophobic interactions. NMR clearly demonstrated that Aβ binding results in the loss of the essential cofactor NAD from the ABAD enzyme. These new data are important for understanding the mechanism of Aβ toxicity and for the search for drugs that disrupt the Aβ-ABAD interaction in Alzheimer disease.

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