The inhibition of trypsin and alpha-chymotrypsin proteolytic activity by aluminum(III)

In Alzheimer's disease, among different hypotheses, amyloid is thought to be formed from a disequilibrium between proteases and protease inhibitors with a consequent production of self-aggregating fragments that are deposited in brain tissues. In this paper we present evidences that aluminum(III) can be a candidate for playing a dismetabolic role in inhibiting the proteolytic activity of the serine proteases trypsin and alpha-chymotrypsin, and the inhibitory reaction can be reversible in the presence of EDTA. The relevance of the physicochemical properties of the metal coordination sphere in this inhibitory effect is also discussed.