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

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 PKCδ-C1B peptide in terms of absolute affinity and the PKCδ-C1A peptide in terms of relative affinity when compared to phorbol-12,13-dibutyrate.