Tuning the Au(I)-mediated inhibition of cathepsin B through ligand substitutions

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Publication Details

Author list: Gunatilleke SS, Barrios AM
Publisher: Elsevier
Publication year: 2008
Journal: Journal of Inorganic Biochemistry (0162-0134)
Volume number: 102
Issue number: 3
Start page: 555
End page: 563
Number of pages: 9
ISSN: 0162-0134
Languages: English-Great Britain (EN-GB)


Abstract

It has been over 80 years since the antiarthritic properties of gold(l) complexes were first recognized. However, a detailed understanding of their mechanism of action has been slow to develop. One likely biological target of gold(l) is the cathepsin family of lysosomal cysteine proteases, enzymes involved in the inflammation and joint destruction that are hallmarks of rheumatoid arthritis (RA). We have previously shown that analogs of auranofin, a clinically available antiarthritic drug, inhibit cathepsin B. In this study, the extent to which the steric and electronic properties of the phosphine ligand can be modified to obtain enhanced potency against cathepsin B is investigated. (C) 2007 Elsevier Inc. All rights reserved.


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Last updated on 2019-23-08 at 11:15