Investigation of proton pump inhibitors binding with bovine serum albumin and their relationship to molecular structure

2012 ◽  
Vol 132 (8) ◽  
pp. 1921-1928 ◽  
Author(s):  
Yuping Zhang ◽  
Shuyun Shi ◽  
Mijun Peng
Vacuum ◽  
2017 ◽  
Vol 136 ◽  
pp. 91-96 ◽  
Author(s):  
Hajar Zarei ◽  
Mostean Bahreinipour ◽  
Khadijeh Eskandari ◽  
Seyed-Ali MousaviZarandi ◽  
Susan Kaboudanian Ardestani

2019 ◽  
Vol 12 (8) ◽  
pp. 3454-3462 ◽  
Author(s):  
Rodrigo S. Correa ◽  
Katia M. Oliveira ◽  
Hiram Pérez ◽  
Ana M. Plutín ◽  
Raúl Ramos ◽  
...  

2017 ◽  
Vol 5 (11) ◽  
pp. 2285-2294 ◽  
Author(s):  
V. H. Giang Phan ◽  
Thavasyappan Thambi ◽  
Bong Sup Kim ◽  
Dai Phu Huynh ◽  
Doo Sung Lee

Highly swellable, dual-responsive bovine serum albumin (BSA)-based injectable hydrogels that exhibit sol-to-gel phase transitions in response to the physiological pH and temperature have been developed.


2019 ◽  
Vol 9 (4) ◽  
pp. 4015-4021

A carrier protein called bovine serum albumin (BSA) interaction with proton-pump inhibitor such as lansoprazole (LSE) has been investigated at 295, 303 and 311 K in pH 7.40 by docking and [UV–vis, CD, FT–IR and fluorescence (emission, 3D and synchronous)] spectroscopic studies. Emission fluorescence has suggested LSE BSA complex formation by static quenching with strong binding. This interaction has proceeded by Vander Waals and hydrogen bonding. An observation from competitive site marker and docking experiments has resulted in binding of LSE with BSA transpired at site II, whereas from Förster’s theory a binding distance ( ) was retrieved to be 0.19 Å from LSE to Trp of BSA. Change in conformation, secondary structure and microenvironment of BSA were noticed after LSE interaction. Diminished binding constant in Zn2+, Na+, Fe2+, Ca2+ and Co2+ ions presence on LSE-BSA interaction was also identified.


Author(s):  
G. D. Gagne ◽  
M. F. Miller

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.


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