Binding of Breviscapine Toward Serum Albumin Studied by Spectroscopic and Electrochemical Techniques.

Abstract:

:Breviscapine, a cerebrovascular drugs extracted from the Chinese herb Erigeron breviscapinus, has been frequently used to clinically treat cerebrovascular diseases such as cerebral thrombosis, cerebral infarction, and cerebral circulation insufficiency. In order to understand its pharmacology or toxicity, the binding mechanism of breviscapine to a model protein, human serum albumin (HSA), was probed by fluorescence, circular dichroism, Fourier transform infrared spectroscopy (FTIR), and electrochemical impedance spectroscopy approaches. The binding affinities and number of the drug with HSA were about 1.73 × 10(4)  M(-1) and 0.99 at 293 K, respectively. The conformation of the protein was slightly altered after interacting with breviscapine. The drug-protein complex was mainly stabilized by electrostatic forces.

journal_name

J Biochem Mol Toxicol

authors

Liu W,Chen Y,Chen H,Zhang Y

doi

10.1002/jbt.21808

subject

Has Abstract

pub_date

2016-09-01 00:00:00

pages

447-54

issue

9

eissn

1095-6670

issn

1099-0461

journal_volume

30

pub_type

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