Study on the binding of puerarin to bovine serum albumin by isothermal titration calorimetry and spectroscopic approaches

2010 ◽  
Vol 102 (1) ◽  
pp. 217-223 ◽  
Author(s):  
Juqun Xi ◽  
Lei Fan
2016 ◽  
Vol 190 ◽  
pp. 173-178 ◽  
Author(s):  
Rachel L. Kilmister ◽  
Peta Faulkner ◽  
Mark O. Downey ◽  
Samuel J. Darby ◽  
Robert J. Falconer

2015 ◽  
Vol 63 (49) ◽  
pp. 10647-10654 ◽  
Author(s):  
Maarit Karonen ◽  
Marianne Oraviita ◽  
Irene Mueller-Harvey ◽  
Juha-Pekka Salminen ◽  
Rebecca J. Green

2017 ◽  
Vol 23 (3) ◽  
pp. 237-243 ◽  
Author(s):  
De-Min Wang ◽  
Xin Meng ◽  
Xiao-Bin Li ◽  
Hao-Jie He ◽  
Teng-Fei Zhao ◽  
...  

AbstractAminophenylboronic acid (ABA) modified bovine serum albumin (BSA) was prepared as neolectin and its interactions with oligosaccharides and glycopolymer were studied by surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC). The conjugation between the primary amine group of the ABA molecule and lysine residues on BSA was performed with an adipate-based strategy to afford the synthetic neoprotein. The number of ABA molecules loaded to BSA surface was determined by matrix-assisted laser desorption/ionization – time of flight (MALDI-TOF) mass spectrometry. In the BSA-ABA and sugar interaction study, no signal was observed for both the SPR and ITC sensor platform using monosaccharides as the analyte, indicating a weak binding affnity, while the galactose modified polymer showed an enhanced response. The binding affinities of the galactosyl-polymer to BSA-ABA from SPR and ITC data were in the micromolar range.


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