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Elucidation of the alpha-keto-aldehyde binding mechanism: a lead structure motif for proteasome inhibition

Gräwert, Melissa Ann, Gallastegui, Nerea, Stein, Martin, Schmidt, Boris, Kloetzel, Peter-Michael, Huber, Robert and Groll, Michael 2011. Elucidation of the alpha-keto-aldehyde binding mechanism: a lead structure motif for proteasome inhibition. Angewandte Chemie - International Edition 50 (2) , pp. 542-544. 10.1002/anie.201005488

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Abstract

Lead role: The role of peptidyl alpha-keto aldehydes as proteasome inhibitors is well established, yet their molecular binding mode requires additional investigation. A cyclization mechanism that proceeds through hemiketal and Schiff base formation with the nucleophilic N-terminal threonine of β5 is shown to result in the reversible formation of a 5,6-dihydro-2H-1,4-oxazine ring. This agent serves as a new lead for the development of anticancer drugs

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > Q Science (General)
Q Science > QD Chemistry
Uncontrolled Keywords: drug discovery; peptidyl glyoxals; proteasomes; reversible inhibition; structure elucidation
Additional Information: Article first published online: 9 DEC 2010
Publisher: Wiley-Blackwell
ISSN: 1433-7851
Last Modified: 24 Jun 2017 08:43
URI: http://orca-mwe.cf.ac.uk/id/eprint/18211

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