title: Improved protein kinase C affinity through final step diversification of a simplified salicylate-derived bryostatin analog scaffold.
abstract: Bryostatin 1, in clinical trials or preclinical development for cancer, Alzheimer's disease, and a first-of-its-kind strategy for HIV/AIDS eradication, is neither readily available nor optimally suited for clinical use. In preceding work, we disclosed a new class of simplified bryostatin analogs designed for ease of access and tunable activity. Here we describe a final step diversification strategy that provides, in only 25 synthetic steps, simplified and tunable analogs with bryostatin-like PKC modulatory activities.
authors.affiliation: Departments of Chemistry and Chemical and Systems Biology, Stanford University , Stanford, California 94305, United States.
authors.forename: Paul A
authors.initials: PA
authors.lastname: Wender
authors.forename: Daryl
authors.initials: D
authors.lastname: Staveness
mesh_terms: D054713:Bryostatins / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D015394:Molecular Structure; D011493:Protein Kinase C / Q000187:drug effects*; D012459:Salicylates / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*
chemical_list: D054713:Bryostatins; D012459:Salicylates; C046785:bryostatin 1; D011493:Protein Kinase C