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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Cysteine protease inhibitors reduce brain β-amyloid and β-secretase activity in vivo and are potential Alzheimer's disease therapeutics

Gregory Hook1 / Vivian Y.H. Hook2 / Mark Kindy3

1American Life Science Pharmaceuticals, Inc., San Diego, CA 92121, USA

2Skaggs School of Pharmacy and Pharmaceutical Sciences, Departments of Neurosciences and Pharmacology, School of Medicine, University of California at San Diego, La Jolla, CA 92093-0657, USA

3Applied Neurotechnology Inc., Charleston, SC 29425, USA

Corresponding author

Citation Information: Biological Chemistry. Volume 388, Issue 9, Pages 979–983, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: 10.1515/BC.2007.117, August 2007

Publication History

Published Online:


β-Secretase inhibitors that lower brain β-amyloid peptides (Aβ) are likely to be effective for treating Alzheimer's disease (AD). Irreversible epoxysuccinyl cysteine protease inhibitors are known to reduce brain Aβ and β-secretase activity in the guinea pig model of human Aβ production. In this study, acetyl-l-leucyl-l-valyl-l-lysinal (Ac-LVK-CHO) is also shown to significantly reduce brain Aβ and β-secretase activity and brain Aβ in the same model. Ac-LVK-CHO is structurally distinct from the epoxysuccinyl inhibitors and is a reversible cysteine protease inhibitor. The results suggest that cysteine protease inhibitors generally, and reversible cysteine protease inhibitors specifically, have potential for development as AD therapeutics.

Keywords: ; Ac-LVK-CHO; Alzheimer's disease; β-amyloid; β-secretase; cathepsin B; cysteine protease; inhibitor

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