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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year

IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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Volume 388, Issue 9 (Sep 2007)


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

Gregory Hook / Vivian Y.H. Hook
  • 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
  • Other articles by this author:
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/ Mark Kindy
Published Online: 2007-08-14 | DOI: https://doi.org/10.1515/BC.2007.117


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

About the article

Corresponding author

Received: 2007-03-12

Accepted: 2007-06-15

Published Online: 2007-08-14

Published in Print: 2007-09-01

Citation Information: Biological Chemistry, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2007.117.

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