Inhibiting prolyl isomerase activity by hybrid organic-inorganic molecules containing rhodium(II) fragments

Jane M Coughlin; Rituparna Kundu; Julian C Cooper; Zachary T Ball

doi:10.1016/j.bmcl.2014.09.068

Inhibiting prolyl isomerase activity by hybrid organic-inorganic molecules containing rhodium(II) fragments

Bioorg Med Chem Lett. 2014 Nov 15;24(22):5203-6. doi: 10.1016/j.bmcl.2014.09.068. Epub 2014 Oct 2.

Authors

Jane M Coughlin¹, Rituparna Kundu¹, Julian C Cooper¹, Zachary T Ball²

Affiliations

¹ Rice University, 6100 Main St, Houston, TX 70005, USA.
² Rice University, 6100 Main St, Houston, TX 70005, USA. Electronic address: zb1@rice.edu.

PMID: 25442313
DOI: 10.1016/j.bmcl.2014.09.068

Abstract

A small molecule containing a rhodium(II) tetracarboxylate fragment is shown to be a potent inhibitor of the prolyl isomerase FKBP12. The use of small molecules conjugates of rhodium(II) is presented as a general strategy for developing new protein inhibitors based on distinct structural and sequence features of the enzyme active site.

Keywords: Enzyme inhibition; FKBP; Metallodrug; Prolyl isomerase; Rhodium.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Enzyme Inhibitors / chemistry*
Enzyme Inhibitors / pharmacology
Peptidylprolyl Isomerase / antagonists & inhibitors
Peptidylprolyl Isomerase / metabolism
Protein Structure, Tertiary
Rhodium / chemistry*
Rhodium / pharmacology
Tacrolimus Binding Protein 1A / antagonists & inhibitors*
Tacrolimus Binding Protein 1A / metabolism

Substances

Enzyme Inhibitors
Rhodium
Tacrolimus Binding Protein 1A
Peptidylprolyl Isomerase