A new structural class of selective and non-covalent inhibitors of the chymotrypsin-like activity of the 20S proteasome

We describe the identification and in vitro characterization of a series of 2-aminobenzylstatine derivatives that inhibit non-covalently the chymotrypsin-like activity of the 20S proteasome. Our initial SAR data demonstrate that the 2-aminobenzylstatine core structure can effectively serve as the basis for designing potent, selective and non-covalent inhibitors of the chymotrypsin-like activity of the 20S proteasome. (C) 2001 Elsevier Science Ltd. All rights reserved.