Photo-induced riboflavin binding to the tryptophan residues of bovine and human serum albumins

1991 ◽  
Vol 30 (2) ◽  
pp. 131-138 ◽  
Author(s):  
G. Tapia ◽  
E. Silva
2014 ◽  
Vol 522-524 ◽  
pp. 337-340
Author(s):  
Yan Qiu Liang ◽  
Ying Zhang

Bovine serum albumin (BSA) and human serum albumin (HSA) interaction with 4-nitroaniline was investigated by fluorescence spectroscopy respectively. 4-Nitroaniline can strongly quench intrinsic fluorescence of BSA and HSA. 4-Nitroaniline exhibits a high affinity to bovine and human serum albumins. The binding constantsKand the number binding sitenwere obtained by double-log regression equation. Negative enthalpy (ΔH) and positive entropy (ΔS) values indicated that both hydrogen bond and hydrophobic forces played a major role in the binding of 4-nitroaniline and SA. The results of synchronous fluorescence showed the polarity around tryptophan residues was decreased and the hydrophobicity was increased.


Soft Matter ◽  
2021 ◽  
Author(s):  
Zhaoyi Wang ◽  
Ningning Zhang ◽  
Jincheng Li ◽  
Jun Lu ◽  
Li Zhao ◽  
...  

Chiral assemblies by combining natural biomolecules with plasmonic nanostructures hold great promise for plasmonic enhanced sensing, imaging, and catalytic applications. Herein, we demonstrate that human serum albumin (HSA) and porcine...


2012 ◽  
Vol 39 (1) ◽  
pp. 371-383 ◽  
Author(s):  
Masaki Nishijima ◽  
Jae-Won Chang ◽  
Cheng Yang ◽  
Gaku Fukuhara ◽  
Tadashi Mori ◽  
...  

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