Development of a Fluorescence Model for the Binding of Medium- to Long-Chain Perfluoroalkyl Acids to Human Serum Albumin Through a Mechanistic Evaluation of Spectroscopic Evidence

2010 ◽  
Vol 82 (15) ◽  
pp. 6463-6471 ◽  
Author(s):  
Paul C. Hebert ◽  
Laura A. MacManus-Spencer
PLoS ONE ◽  
2017 ◽  
Vol 12 (6) ◽  
pp. e0180404 ◽  
Author(s):  
Keishi Yamasaki ◽  
Saya Hyodo ◽  
Kazuaki Taguchi ◽  
Koji Nishi ◽  
Noriyuki Yamaotsu ◽  
...  

1989 ◽  
Vol 258 (1) ◽  
pp. 199-204 ◽  
Author(s):  
B Honoré ◽  
A O Pedersen

pH- and fatty acid-induced conformational changes in human serum albumin were investigated by fluorescence-energy transfer, determining the distance between Trp-214 and bound bilirubin at 25 degrees C. This distance changes significantly with the pH, being 2.52 +/- 0.01 nm at pH 6, 2.31 +/- 0.04 nm at pH 9, 2.13 +/- 0.07 nm at pH 11.0 and 2.77 nm at pH 11.9. The influence of different fatty acids on the distance was also determined. At pH 7.4 medium-chain fatty acids seem to increase this distance, whereas long-chain fatty acids, at low concentrations, decrease the distance between the two chromophores. The contraction of the protein carrying long-chain saturated fatty acids is even more pronounced at pH 9.


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