Tenellones A and B from a Diaporthe sp.: two highly substituted benzophenone inhibitors of parasite cGMP-dependent protein kinase activity

Chaowei Zhang; John G Ondeyka; Kithsiri B Herath; Ziqiang Guan; Javier Collado; Gonzalo Platas; Fernando Pelaez; Penny S Leavitt; Anne Gurnett; Bakela Nare; Paul Liberator; Sheo B Singh

doi:10.1021/np049591n

Tenellones A and B from a Diaporthe sp.: two highly substituted benzophenone inhibitors of parasite cGMP-dependent protein kinase activity

J Nat Prod. 2005 Apr;68(4):611-3. doi: 10.1021/np049591n.

Authors

Chaowei Zhang¹, John G Ondeyka, Kithsiri B Herath, Ziqiang Guan, Javier Collado, Gonzalo Platas, Fernando Pelaez, Penny S Leavitt, Anne Gurnett, Bakela Nare, Paul Liberator, Sheo B Singh

Affiliation

¹ Natural Products Chemistry and Human and Animal Infectious Disease, Merck Research Laboratories, P.O. Box 2000, Rahway, New Jersey 07065, USA.

PMID: 15844962
DOI: 10.1021/np049591n

Abstract

Parasite cGMP-dependent protein kinase (PKG) has been recently validated as a biochemical target for the treatment of coccidiosis. To discover new anticoccidial leads, we have screened our library of natural product extracts for inhibitors of parasite PKG. Bioassay-guided fractionation of the microbial extracts has led to the discovery of tenellones A (2) and B (3), two new highly substituted benzophenones. The isolation, structure, and activity of these compounds are described.

MeSH terms

Animals
Benzophenones / chemistry
Benzophenones / isolation & purification*
Benzophenones / pharmacology
Cyclic GMP-Dependent Protein Kinases
Enzyme Inhibitors / chemistry
Enzyme Inhibitors / isolation & purification*
Enzyme Inhibitors / pharmacology
Fungi / chemistry*
Molecular Structure
Plants, Medicinal / chemistry
Spain
Toxoplasma / metabolism

Substances

Benzophenones
Enzyme Inhibitors
tenellone A
tenellone B
Cyclic GMP-Dependent Protein Kinases