Structure−Activity Relationship Studies of Ethyl 2-Amino-6-bromo-4-(1-cyano-2-ethoxy-2-oxoethyl)-4H-chromene-3-carboxylate (HA 14-1), an Antagonist for Antiapoptotic Bcl-2 Proteins To Overcome Drug Resistance in Cancer

Journal of Medicinal Chemistry
2006.0

Abstract

The structure-activity relationship studies of ethyl 2-amino-6-cyclopentyl-4-(1-cyano-2-ethoxy-2-oxoethyl)-4H-chromene-3-carboxylate (1, HA 14-1), an antagonist of the antiapoptotic Bcl-2 proteins, are reported. A series of analogues of 1 with varied functional groups at the 6-position of the chromene ring were synthesized. These candidates were evaluated for their binding interactions with three antiapoptotic proteins: Bcl-2, Bcl-XL, and Bcl-w. They were also assayed for their in vitro cytotoxicities against a set of Jurkat cells with varied levels of Bcl-2 and Bcl-XL proteins and a non-small-cell lung carcinoma cell line (NCI-H460). It was found that the 6-bromo of 1 was not essential for its bioactivity and the 6-position can accommodate a variety of alkyl groups. 1 and its analogues bind to all of the three antiapoptotic Bcl-2 proteins tested. Positive correlations were observed between the binding affinities of these candidates to the antiapoptotic Bcl-2 proteins and their in vitro cytotoxicities, suggesting that the antiapoptotic Bcl-2 proteins are likely to be the cellular targets of 1 and its analogues. (In this study, the binding interactions of the small molecules to antiapoptotic Bcl-2 proteins were studied by assaying their abilities to compete against a Bak peptide binding to the antiapoptotic Bcl-2 proteins. Inhibitory constants, instead of dissociation constants, were obtained in such assays. The term "binding affinity" is used in this article for simplicity.) The most active compound, 3g, had a >3-fold increase of binding affinity to the antiapoptotic Bcl-2 proteins and a >13-fold increase of in vitro cytotoxicity over 1. Though Jurkat cells with transgenic overexpression of Bcl-2 or Bcl-XL protein can develop resistance to standard cancer therapies, such cells failed to develop resistance to 1 based candidates. 1 also sensitizes Jurkat cells to cisplatin. These studies provide further support that 1 and its analogues function as antagonists for antiapoptotic Bcl-2 proteins and that they have the potential, either as a single agent or as a combination therapy with other anticancer agents, to treat cancers with the overexpression of antiapoptotic Bcl-2 proteins.

Knowledge Graph

Similar Paper

Structure−Activity Relationship Studies of Ethyl 2-Amino-6-bromo-4-(1-cyano-2-ethoxy-2-oxoethyl)-4H-chromene-3-carboxylate (HA 14-1), an Antagonist for Antiapoptotic Bcl-2 Proteins To Overcome Drug Resistance in Cancer
Journal of Medicinal Chemistry 2006.0
Structure−Activity Relationship and Molecular Mechanisms of Ethyl 2-Amino-4-(2-ethoxy-2-oxoethyl)-6-phenyl-4H-chromene-3-carboxylate (sHA 14-1) and Its Analogues
Journal of Medicinal Chemistry 2009.0
Design of Bcl-2 and Bcl-xL Inhibitors with Subnanomolar Binding Affinities Based upon a New Scaffold
Journal of Medicinal Chemistry 2012.0
Structure-Based Design of Potent Bcl-2/Bcl-xL Inhibitors with Strong in Vivo Antitumor Activity
Journal of Medicinal Chemistry 2012.0
Pyrogallol-Based Molecules as Potent Inhibitors of the Antiapoptotic Bcl-2 Proteins
Journal of Medicinal Chemistry 2007.0
Discovery of Small-Molecule Inhibitors of Bcl-2 through Structure-Based Computer Screening
Journal of Medicinal Chemistry 2001.0
Dual inhibitors of the pro-survival proteins Bcl-2 and Mcl-1 derived from natural compound meiogynin A
European Journal of Medicinal Chemistry 2018.0
Design, synthesis, and activity evaluation of selective inhibitors of anti-apoptotic Bcl-2 proteins: The effects on the selectivity of the P1 pockets in the active sites
Bioorganic & Medicinal Chemistry Letters 2016.0
Studies Leading to Potent, Dual Inhibitors of Bcl-2 and Bcl-xL
Journal of Medicinal Chemistry 2007.0
Structure-based design of rhodanine-based acylsulfonamide derivatives as antagonists of the anti-apoptotic Bcl-2 protein
Bioorganic & Medicinal Chemistry 2012.0