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Wiley, ChemMedChem, 10(5), p. 1701-1705, 2010

DOI: 10.1002/cmdc.201000293

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20S proteasome inhibition: designing noncovalent linear peptide mimics of the natural product TMC-95A.

Journal article published in 2010 by Michael Groll, Nerea Gallastegui, Xavier Maréchal, Virginie Le Ravalec, Nicolas Basse, Nicolas Richy, Emilie Genin, Robert Huber, Luis Moroder ORCID, Joëlle Vidal ORCID, Michèle Reboud-Ravaux
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

The 20S proteasome maintains homeostasis and regulates important intracellular processes by subjecting most intracellular proteins to endoproteolytic cleavage. This complex hydrolysis machinery has received considerable attention for the treatment of many diseases, including cancer. We report a new set of noncovalent peptide mimics based on TMC-95A and our rational approach to inhibitor optimization using both crystallographic and kinetic studies.