S100B is a protein found at 20-times greater abundance in Alzheimer's diseased (AD) brains versus controls and it regulates the activities of its protein targets based on its metal content.  For example, zinc-bound S100B binds to tau, thereby promoting its hyperphosphorylation, which ultimately results in the formation of neurofibrillary tangles and cellular deterioration in AD.  Less is known about target protein regulation by copper(II)-bound S100B, but this metal has been shown to catalyze the formation of a disulfide bond between the two S100B monomers during the binding process.  Therefore, the conformational changes imposed on S100B by copper likely affect protein function, so a detailed characterization of the binding event between copper and S100B will be valuable to the pharmaceutical industry.  We describe investigations into metal binding using isothermal titration calorimetry and electron paramagnetic resonance spectroscopy toward this end.

Copper binding to S100B

239th National Meeting (2010)

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