The C4 hydroxyl group of phorbol esters is not necessary for protein kinase C binding

Minoru Tanaka, Kazuhiro Irie, Yu Nakagawa, Yoshimasa Nakamura, Hajime Ohigashi, Paul A. Wender

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

To investigate the role of the hydroxyl group at position 4 of the phorbol esters in protein kinase C (PKC) binding and function. 4β-deoxy-phorbol-12,13-dibutyrate (4β-deoxy-PDBu, 5a) and 4β-deoxy-phorbol-13-acetate (6a) were synthesized from phorbol (1). The binding affinities of these 4β-deoxy compounds (5a, 6a) to the 13 PKC isozyme C1 domains were quite similar to those of the corresponding 4β-hydroxy compounds (4a. 4b). suggesting that the C4 hydroxyl group of phorbol esters is not necessary for PKC binding. Moreover. functional assays showed that 4β-deoxy-PDBu (5a) exhibited biological activities (Epstein-Barr virus induction and superoxide generation) equally potent to those of PDBu (4a). These solution phase results differ from expectations based on the previously reported solid-phase structure of the complex of PKCδ-C1B and phorbol-13-acetate (4b).

Original languageEnglish
Pages (from-to)719-722
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume11
Issue number5
DOIs
Publication statusPublished - Mar 12 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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