Inhibition of protein kinase C by cationic amphiphiles

Biochemistry. 1992 Sep 22;31(37):9025-30. doi: 10.1021/bi00152a045.

Abstract

A large number of PKC inhibitors are positively charged. We evaluated the structural features of cationic amphiphiles which are necessary for inhibiting PKC. Many of these compounds were derivatives of cholesterol, which possesses a hydrophobic backbone which does not perturb hydrocarbon packing in membrane bilayers. In addition, they contain a tertiary or quaternary nitrogen functionality in the head group. All designed cholesterol-based amphiphiles inhibit PKC activity; the potency of the amphiphile correlates with the presence of positive charge. Quaternary ammonium amphiphiles are 10-fold more potent than their tertiary amine counterparts, generally inhibiting in the 10-60 microM range using the Triton mixed micelle assay. Aside from charge, factors such as the structure of the amine-containing head group, its length from the hydrocarbon moiety, or the number of amine groups on the amphiphile did not markedly influence inhibitor potency. In contrast, the hydrocarbon backbone did influence potency: cationic amphiphiles containing a steroid backbone were more potent inhibitors of PKC than their straight-chain analogues. Changing the nature of the hydrocarbon from a sterol to an alkyl group lowers the pK of the amine head group so that the straight-chain analogues are no longer cationic in the conditions in the PKC assay. The results of these studies suggest that a combination of positive charge and a bilayer-stabilizing structural characteristic provides a basis for the rational design of PKC inhibitors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain / enzymology
  • Calorimetry, Differential Scanning
  • Cations / chemistry
  • Drug Design
  • Hydrogen-Ion Concentration
  • Lipid Bilayers / chemistry
  • Micelles
  • Protein Kinase C / antagonists & inhibitors*
  • Rats
  • Steroids / chemistry
  • Structure-Activity Relationship

Substances

  • Cations
  • Lipid Bilayers
  • Micelles
  • Steroids
  • Protein Kinase C