Selective binding of bryostatin analogues to the cysteine rich domains of protein kinase C isozymes

Bioorg Med Chem Lett. 1999 Jun 21;9(12):1687-90. doi: 10.1016/s0960-894x(99)00263-2.

Abstract

Designed bryostatin analogues are assayed for binding affinity to individual cysteine rich domains of several protein kinase C (PKC) isozymes. These analogues exhibit significant selectivity for the PKCdelta-C1B peptide in terms of absolute affinity and the PKCdelta-C1A peptide in terms of relative affinity when compared to phorbol-12,13-dibutyrate.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / metabolism*
  • Binding, Competitive
  • Bryostatins
  • Cysteine / metabolism*
  • Enzyme Activation
  • Humans
  • Isoenzymes / metabolism*
  • Lactones / chemistry
  • Lactones / metabolism*
  • Macrolides
  • Protein Conformation
  • Protein Kinase C / chemistry
  • Protein Kinase C / metabolism*
  • Protein Kinase C-delta
  • Tumor Cells, Cultured

Substances

  • Antineoplastic Agents
  • Bryostatins
  • Isoenzymes
  • Lactones
  • Macrolides
  • bryostatin 1
  • PRKCD protein, human
  • Protein Kinase C
  • Protein Kinase C-delta
  • Cysteine