Published in

American Chemical Society, Journal of Medicinal Chemistry, 5(53), p. 2319-2323, 2010

DOI: 10.1021/jm9015685

Links

Tools

Export citation

Search in Google Scholar

Incorporation of Fluorinated Phenylalanine Generates Highly Specific Inhibitor of Proteasome's Chymotrypsin-like Sites

Journal article published in 2010 by Paul P. Geurink, Nora Liu, Michiel P. Spaans, Sondra L. Downey, Adrianus M. C. H. van den Nieuwendijk, Gijsbert A. van der Marel, Alexei F. Kisselev, Bogdan I. Florea ORCID, Herman S. Overkleeft ORCID
This paper is available in a repository.
This paper is available in a repository.

Full text: Download

Green circle
Preprint: archiving allowed
  • Must obtain written permission from Editor
  • Must not violate ACS ethical Guidelines
Upload
Orange circle
Postprint: archiving restricted
  • Must obtain written permission from Editor
  • Must not violate ACS ethical Guidelines
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

Abstract

Proteasomal processing is conducted by three individual catalytic subunits, namely beta1, beta2, and beta5. Subunit-specific inhibitors are useful tools in dissecting the role of these individual subunits and are leads toward the development of antitumor agents. We here report that the presence of fluorinated phenylalanine derivatives in peptide based proteasome inhibitors has a profound effect on inhibitor potency and selectivity. Specifically, compound 4a emerges as one of the most beta5 specific inhibitors known to date.