Improved Protein Kinase C Affinity through Final Step Diversification of a Simplified Salicylate-Derived Bryostatin Analog Scaffold | Zendy

Paul A. Wender | Zendy; Daryl Staveness | Zendy

Open Access

Improved Protein Kinase C Affinity through Final Step Diversification of a Simplified Salicylate-Derived Bryostatin Analog Scaffold

Author(s) -

Paul A. Wender,

Daryl Staveness

Publication year - 2014

Publication title -

organic letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.94

H-Index - 239

eISSN - 1523-7060

pISSN - 1523-7052

DOI - 10.1021/ol502492b

Subject(s) - bryostatin 1 , chemistry , protein kinase c , scaffold , scaffold protein , kinase , combinatorial chemistry , computational biology , biochemistry , signal transduction , computer science , biology , database

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.

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