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.
Centro CNR per lo Studio della Biochimica, Università di Padova, Italy.
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Zatta
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Bordin
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Favarato
D000535:Aluminum / Q000737:chemistry / Q000494:pharmacology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D004492:Edetic Acid / Q000494:pharmacology; D007700:Kinetics; D014357:Trypsin / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000494:pharmacology*
D014361:Trypsin Inhibitors; D004492:Edetic Acid; D000535:Aluminum; D002918:Chymotrypsin; D014357:Trypsin