EMAIL THIS PAGE TO A FRIEND

Chemical biology & drug design

Binding and Anticancer Properties of Plumbagin with Human Serum Albumin.


PMID 25534036

Abstract

Plumbagin has received extensive attention as a promising anticancer drug. Therefore, we investigated the binding and anticancer properties of plumbagin with human serum albumin. Fluorescence results demonstrated that plumbagin interacts with human serum albumin, although its binding affinity may be affected to various extents by different compounds. The human serum albumin-plumbagin complex structure revealed that plumbagin binds to the hydrophobic cavity in the IIA subdomain of human serum albumin through hydrogen bonding and hydrophobic interactions. The plumbagin-human serum albumin complex enhances cytotoxicity by 2- to 3-fold particularly in cancer cells but has no effect on normal cells in vitro. Compared with the unbound drug, the human serum albumin-plumbagin complex promotes HeLa cell apoptosis and has a stronger capacity for cell cycle arrest at the G2/M phase of HeLa cells. In conclusion, this study contributes to the rational design and development of plumbagin-based drugs and a drug-human serum albumin delivery system.

Related Materials

Product #

Image

Description

Molecular Formula

Add to Cart

P7262
Plumbagin from Plumbago indica
C11H8O3
S5375
Shikimic acid, ≥99%
C7H10O5