Interactions of different polyphenols with bovine serum albumin using fluorescence quenching and molecular docking

2012 ◽  
Vol 135 (4) ◽  
pp. 2418-2424 ◽  
Author(s):  
Mihaela Skrt ◽  
Evgen Benedik ◽  
Črtomir Podlipnik ◽  
Nataša Poklar Ulrih
Luminescence ◽  
2009 ◽  
pp. n/a-n/a ◽  
Author(s):  
U. S. Mote ◽  
S. L. Bhattar ◽  
S. R. Patil ◽  
G. B. Kolekar

2021 ◽  
Vol 11 (5) ◽  
pp. 13102-13110

Novel (4R,12aS)-7-methoxy-4-methyl-6,8-dioxo-3,4,6,8,12,12a-hexahydro-2H-pyrido-[1',2':-4,5]-pyrazino[2,1-b][1,3]oxazine-9-carboxylic acid (L) was synthesized and characterised. The interaction between bovine serum albumin (BSA) with L was scrutinized by steady-state fluorescence spectroscopy, fluorescence anisotropy, fluorescence lifetime, and molecular docking methods. The fluorescence titration experiments of BSA resulted in fluorescence quenching with the incremental addition of L. The conformational binding of L to BSA has been investigated by molecular docking analysis. The molecular probe's best conformation showed the affinity as free binding energy release of -7.93 Kcal/mol. The docking analysis confirms that ligand binds in the near vicinity of TRP-213 in the binding pocket of subdomain IIA.


Bioimpacts ◽  
2017 ◽  
Vol 7 (4) ◽  
pp. 241-246 ◽  
Author(s):  
Yousef Sohrabi ◽  
Vahid Panahi-Azar ◽  
Abolfazl Barzegar ◽  
Jafar Ezzati Nazhad Dolatabadi ◽  
Parvin Dehghan

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