Studies on the binding behavior of prodigiosin with bovine hemoglobin by multi-spectroscopic techniques.
In this article, the interaction mechanism of prodigiosin (PG) with bovine hemoglobin (BHb) is studied in detail using various spectroscopic technologies. UV-vis absorption and fluorescence spectra demonstrate the interaction process. The Stern-Volmer plot and the time-resolved fluorescence study suggest the quenching mechanism of fluorescence of BHb by PG is a static quenching procedure, and the hydrophobic interactions play a major role in binding of PG to BHb. Furthermore, synchronous fluorescence studies, Fourier transform infrared (FTIR) and circular dichroism (CD) spectra reveal that the conformation of BHb is changed after conjugation with PG.
College of Chemistry and Materials Science, Analysis and Testing Center, Jiangsu Key Laboratory of Biofunctional Materials, Nanjing Normal University, Nanjing 210046, PR China.
Jing
J
Tang
Chao
C
Yang
Lin
L
Zhou
Fei
F
Ma
Shuchao
S
Liu
Shaohua
S
Wei
Jiahong
J
Zhou
Yanhuai
Y
Zhou
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D006454:Hemoglobins / Q000378:metabolism*; D007700:Kinetics; D008968:Molecular Conformation; D011353:Prodigiosin / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D013997:Time Factors
D006454:Hemoglobins; D011353:Prodigiosin