Synthesis and biological evaluation of structurally diverse α-conformationally restricted chalcones and related analogues.

ABSTRACT: Numerous members of the combretastatin and chalcone families of natural products function as inhibitors of tubulin polymerization through a binding interaction at the colchicine site on β-tubulin. These molecular scaffolds inspired the development of many structurally modified derivatives and analogues as promising anticancer agents. A productive design blueprint that involved molecular hybridization of the pharmacophore moieties of combretastatin A-4 (CA4) and the chalcones led to the discovery of two promising lead molecules referred to as KGP413 and SD400. The corresponding water-soluble phosphate prodrug salts of KGP413 and SD400 selectively damaged tumor-associated vasculature, thus highlighting the potential development of these molecules as vascula

SUBMITTER: Maguire CJ 

PROVIDER: S-EPMC6734540 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature