TY - JOUR
T1 - Spectroscopic investigation on the interaction of hyperbranched poly (amine) ester with model plasma protein
T2 - Effect on the structural and conformational changes
AU - Xiao, Fengjuan
AU - Gu, Muqing
AU - Liang, Ye
AU - Li, Lanlan
AU - Luo, Yunjun
PY - 2014
Y1 - 2014
N2 - Mechanism of interaction between hyperbranched poly (amine) ester (HPAE) and bovine serum albumin (BSA) was investigated using fluorescence, synchronous fluorescence, three-dimensional fluorescence spectra, UV-Vis spectrometry and circular dichroism (CD). The structural and conformational changes of BSA induced by HPAE were also revealed in this study. Stern-Volmer analysis of fluorescence quenching showed that BSA fluorescence was statically quenched by HPAE, which implied that ground state complex formed between BSA and HPAE. Vander Waals force and hydrogen bond played major roles in the interaction of HPAE with BSA. The distance, r between the donor (BSA) and acceptor (HPAE) was calculated based on the Forster's theory of non-radiation energy transfer and was found to be 3.24 nm. Synchronous and three-dimensional fluorescence studies showed that the interaction of BSA with HPAE induced conformational changes in BSA. The secondary structural analysis by CD spectra suggested that HPAE binding induced BSA to form a more compact conformation with about 6.9% transformation of α-helix to β-sheet. Molecular model of the interaction of HPAE with BSA was also presented according to the results of this study.
AB - Mechanism of interaction between hyperbranched poly (amine) ester (HPAE) and bovine serum albumin (BSA) was investigated using fluorescence, synchronous fluorescence, three-dimensional fluorescence spectra, UV-Vis spectrometry and circular dichroism (CD). The structural and conformational changes of BSA induced by HPAE were also revealed in this study. Stern-Volmer analysis of fluorescence quenching showed that BSA fluorescence was statically quenched by HPAE, which implied that ground state complex formed between BSA and HPAE. Vander Waals force and hydrogen bond played major roles in the interaction of HPAE with BSA. The distance, r between the donor (BSA) and acceptor (HPAE) was calculated based on the Forster's theory of non-radiation energy transfer and was found to be 3.24 nm. Synchronous and three-dimensional fluorescence studies showed that the interaction of BSA with HPAE induced conformational changes in BSA. The secondary structural analysis by CD spectra suggested that HPAE binding induced BSA to form a more compact conformation with about 6.9% transformation of α-helix to β-sheet. Molecular model of the interaction of HPAE with BSA was also presented according to the results of this study.
KW - Circular dichroism
KW - Conformational change
KW - Hyperbranched poly (amine) ester
KW - Model plasma protein
KW - Three-dimensional fluorescence
UR - http://www.scopus.com/inward/record.url?scp=84886168621&partnerID=8YFLogxK
U2 - 10.1016/j.saa.2013.09.074
DO - 10.1016/j.saa.2013.09.074
M3 - Article
C2 - 24161873
AN - SCOPUS:84886168621
SN - 1386-1425
VL - 118
SP - 1106
EP - 1112
JO - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
JF - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
ER -