Literature DB >> 10074468

Molecular forceps from combinatorial libraries prevent the farnesylation of Ras by binding to its carboxyl terminus.

D L Dong1, R Liu, R Sherlock, M H Wigler, H P Nestler.   

Abstract

INTRODUCTION: Ras is one of the major oncogenes. In order to function properly it has to undergo post-translational processing at its carboxyl terminus. It has been shown that inhibitors of farnesyl transferase, the first enzyme in the processing chain, can suppress the transforming activity of oncogenic Ras.
RESULTS: We have identified molecular forceps, branched peptidic molecules, from combinatorial libraries that bind to the carboxyl terminus of Ras and interfere with its farnesylation without inhibiting the farnesyl transferase. The active molecules were selected by a screening against the carboxy-terminal octapeptide of Ras.
CONCLUSIONS: The implications of our findings are twofold. First, we demonstrate that it is possible to prevent enzymatic transformations by blocking the enzyme's access to its substrate using a synthetic small molecule to mask the substrate. Second, we show that it is feasible to derive molecules from combinatorial libraries that bind a specific epitope on a protein by selecting these molecules with the isolated peptide epitope.

Mesh:

Substances:

Year:  1999        PMID: 10074468     DOI: 10.1016/S1074-5521(99)89005-X

Source DB:  PubMed          Journal:  Chem Biol        ISSN: 1074-5521


  3 in total

Review 1.  Protein-Catalyzed Capture Agents.

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Journal:  Nature       Date:  2008-06-12       Impact factor: 49.962

3.  Sequence-Selective Covalent CaaX-Box Receptors Prevent Farnesylation of Oncogenic Ras Proteins and Impact MAPK/PI3 K Signaling.

Authors:  Matthias Franz; Britta Mörchen; Carsten Degenhart; Daniel Gülden; Oleksandr Shkura; Dirk Wolters; Uwe Koch; Bert Klebl; Raphael Stoll; Iris Helfrich; Jürgen Scherkenbeck
Journal:  ChemMedChem       Date:  2021-05-19       Impact factor: 3.466

  3 in total

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