Structure activity relationship study of curcumin analogues toward the amyloid-beta aggregation inhibitor

Hitoshi Endo; Yuri Nikaido; Mamiko Nakadate; Satomi Ise; Hiroyuki Konno

doi:10.1016/j.bmcl.2014.10.076

Structure activity relationship study of curcumin analogues toward the amyloid-beta aggregation inhibitor

Bioorg Med Chem Lett. 2014 Dec 15;24(24):5621-5626. doi: 10.1016/j.bmcl.2014.10.076. Epub 2014 Oct 30.

Authors

Hitoshi Endo¹, Yuri Nikaido¹, Mamiko Nakadate¹, Satomi Ise¹, Hiroyuki Konno²

Affiliations

¹ Department of Biochemical Engineering, Graduate School of Science and Technology, Yamagata University, Yonezawa, Yamagata 992-8510, Japan.
² Department of Biochemical Engineering, Graduate School of Science and Technology, Yamagata University, Yonezawa, Yamagata 992-8510, Japan. Electronic address: konno@yz.yamagata-u.ac.jp.

PMID: 25467149
DOI: 10.1016/j.bmcl.2014.10.076

Abstract

Inhibition of the amyloid β aggregation process could possibly prevent the onset of Alzheimer's disease. In this article, we report a structure-activity relationship study of curcumin analogues for anti amyloid β aggregation activity. Compound 7, the ideal amyloid β aggregation inhibitor in vitro among synthesized curcumin analogues, has not only potent anti amyloid β aggregation effects, but also water solubility more than 160 times that of curcumin. In addition, new approaches to improve water solubility of curcumin-type compounds are proposed.

Keywords: Aggregation inhibitor; Alzheimer’s disease; Amyloid-beta; Curcumin; Water solubility.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amyloid beta-Peptides / antagonists & inhibitors*
Amyloid beta-Peptides / metabolism
Curcumin / chemical synthesis
Curcumin / chemistry*
Humans
Kinetics
Molecular Conformation
Protein Binding
Quantum Theory
Solubility
Structure-Activity Relationship

Substances

Amyloid beta-Peptides
Curcumin