Stable analogues of geranylgeranyl diphosphate possessing improved geranylgeranyl versus farnesyl protein transferase inhibitory selectivity

Autor:	Simone Bertini, Chiara Papi, Filippo Minutolo, Silvia Barontini, Giorgio Placanica, Marco Macchia, Laura Betti, Romano Danesi, Gino Giannaccini, Gianbattista Gervasi, Simona Rapposelli
Rok vydání:	2003
Předmět:	Models Molecular Farnesyl Protein Transferase Stereochemistry medicine.drug_class Clinical Biochemistry Pharmaceutical Science Carboxamide Biochemistry Substrate Specificity Structure-Activity Relationship Geranylgeranylation Polyisoprenyl Phosphates Drug Discovery medicine Transferase Moiety Enzyme Inhibitors Molecular Biology chemistry.chemical_classification Alkyl and Aryl Transferases Molecular Structure biology Organic Chemistry Terpenoid Kinetics Enzyme chemistry Enzyme inhibitor biology.protein Molecular Medicine Diterpenes
Zdroj:	Bioorganic & Medicinal Chemistry Letters. 13:4405-4408
ISSN:	0960-894X
Popis:	Phosphonoacetamido(oxy) groups have proven to be good mimics of the diphosphate portion in geranylgeranyl protein transferase I (GGTase I) inhibitors. The introduction of small alkyl groups (Me, Et) into the diphosphate mimic moiety caused a further decrease in collateral farnesyl protein transferase (FTase) inhibitory activity, thereby improving GGTase I over FTase selectivity.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f625047d63dddda60434703e1c50c7f https://doi.org/10.1016/j.bmcl.2003.09.035 Zobrazit plný text záznamu Full Text from ScienceDirect