Modulation of Accessibility of Subdomain IB in the pH-Dependent Interaction of Bovine Serum Albumin with Cochineal Red A: A Combined View from Spectroscopy and Docking Simulations#

2013 ◽  
Vol 61 (19) ◽  
pp. 4606-4613 ◽  
Author(s):  
Priyanka Bolel ◽  
Niharendu Mahapatra ◽  
Shubhashis Datta ◽  
Mintu Halder
Molecules ◽  
2019 ◽  
Vol 24 (20) ◽  
pp. 3667
Author(s):  
Yasuyuki Fujii ◽  
Yoshitomo Suhara ◽  
Yusuke Sukikara ◽  
Tomohiro Teshima ◽  
Yoshihisa Hirota ◽  
...  

Flavan-3-ols (FLs), specifically catechin and its oligomer B-type procyanidins, are suggested to potently bind to bovine serum albumin (BSA). We examined the interaction between BSA and FLs by fluorescence quenching and found the following order of binding activities to BSA: cinnamtannin A2 (A2; tetramer) > procyanidin C1 (C1; trimer) ≈ procyanidin B2 (B2, dimer) > (−)epicatechin (EC, monomer). Docking simulations between BSA and each compound at the binding site showed that the calculated binding energies were consistent with the results of our experimental assay. FLs exerted cytotoxicity at 1000 μg/mL in F11 cell culture with fetal bovine serum containing BSA. In culture containing serum-free medium, FLs exhibited significant cell proliferation at 10−4 μg/mL and cytotoxicity was observed at concentrations greater than 10 μg/mL. Results of this study suggest that interactions between polyphenols and BSA should be taken into account when evaluating procyanidin in an in vitro cell culture system.


Luminescence ◽  
2014 ◽  
Vol 30 (2) ◽  
pp. 240-246 ◽  
Author(s):  
Qing Wang ◽  
Jiawei He ◽  
Jin Yan ◽  
Di Wu ◽  
Hui Li

1985 ◽  
Vol 145 (2) ◽  
pp. 217-221 ◽  
Author(s):  
Athar Husain ◽  
Geoffrey J. Howlett ◽  
William H. Sawyer

1986 ◽  
Vol 7 (10) ◽  
pp. 447-453
Author(s):  
Adam Csordas ◽  
Peter Josef Oefner ◽  
Georg Bartsch ◽  
Hans Grunicke ◽  
Giancarlo Lancini

1976 ◽  
Vol 71 (2) ◽  
pp. 666-669 ◽  
Author(s):  
R Rodewald

Rat and rabbit IgG immunoglobulins conjugated to horseradiah peroxidase as a histochemical marker bind at 0 degrees C to the luminal surface of absorptive cells in isolated segments of jejunum from 10-12-day old rats. Binding is observed at pH 6.0, near the normal luminal pH of the duodenum and jejunum at this age, but not at pH 7.4. Furthermore, no binding occurs when cells are exposed at pH 6.0 to either free peroxidase or peroxidase conjugated to chicken or sheep IgG immunoglobulins or bovine serum albumin. The sensitivity of binding to pH suggests a means whereby immunoglobulins which are selectively absorbed by the cells can be released efficiently at the abluminal surface.


2007 ◽  
Vol 127 (2) ◽  
pp. 515-522 ◽  
Author(s):  
Dejiang Gao ◽  
Yuan Tian ◽  
Fanghui Liang ◽  
Danhong Jin ◽  
Yanhua Chen ◽  
...  

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