Spectroscopic Investigation on the Interaction of a Cyanine Dye with Serum Albumins

The interactions of a cyanine dye with human serum albumin (HSA) and bovine serum albumin (BSA) have been investigated by using absorption and fluorescence spectra. Absorption spectral studies show that binding to the serum albumins leads to a bathochromic shift of the monomer band together with a n...

Full description

Saved in:
Bibliographic Details
Published in:Chinese journal of chemistry 2008-02, Vol.26 (2), p.397-401
Main Authors: ZHANG, Ya-Zhou, YANG, Qian-Fan, DU, Hong-Yan, TANG, Ya-Lin, XU, Guang-Zhi, YAN, Wen-Peng
Format: Article
Language:English
Subjects:
bovine serum albumin
cyanine dye
fluorescent probe
human serum albumin
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The interactions of a cyanine dye with human serum albumin (HSA) and bovine serum albumin (BSA) have been investigated by using absorption and fluorescence spectra. Absorption spectral studies show that binding to the serum albumins leads to a bathochromic shift of the monomer band together with a notable intensity change. Furthermore, the number of binding sites (n) was identified by the absorption spectra. There is a constant enhancement of fluorescence quantum yield when the cyanine dye complexes with HSA or BSA. The apparent binding constant (Ka) and the free energy changes (ΔG) were obtained by analysis of fluorescence data of the cyanine dye in the absence and presence of HSA and BSA. Compared to BSA, HSA associates with the dye in a stronger way.
ISSN:1001-604X
1614-7065
DOI:10.1002/cjoc.200890076