scholarly journals Synthesis and structural studies of 16‐ferrocenemethyl‐estra‐1,3,5(10)‐triene‐3,17β‐diol and its interaction with human serum albumin by fluorescence spectroscopy and in silico docking approaches

2020 ◽  
Vol 34 (4) ◽  
Author(s):  
José A. Carmona‐Negrón ◽  
José M. Liboy‐Lugo ◽  
Alberto Santana ◽  
Enrique Meléndez

2021 ◽  
pp. 116888
Author(s):  
Fahad A. Alhumaydhi ◽  
Mohammad Abdullah Aljasir ◽  
Abdullah S.M. Aljohani ◽  
Suliman A. Alsagaby ◽  
Ameen S.S. Alwashmi ◽  
...  


2020 ◽  
Vol 303 ◽  
pp. 112648 ◽  
Author(s):  
Md. Zahirul Kabir ◽  
Zineddine Benbekhti ◽  
Nor Farrah Wahidah Ridzwan ◽  
Rabiâa Merrouche ◽  
Noureddine Bouras ◽  
...  






2011 ◽  
Vol 27 (1) ◽  
pp. 79-84 ◽  
Author(s):  
Feng GE ◽  
Lixiang JIANG ◽  
Diqiu LIU ◽  
Chaoyin CHEN


2006 ◽  
Vol 46 (6) ◽  
pp. 2709-2724 ◽  
Author(s):  
Ernesto Estrada ◽  
Eugenio Uriarte ◽  
Enrique Molina ◽  
Yamil Simón-Manso ◽  
George W. A. Milne


2021 ◽  
Vol 28 ◽  
Author(s):  
Priyadarshini ◽  
Abhishek Negi ◽  
Chetna Faujdar ◽  
Lokesh Nigam ◽  
Naidu Subbarao

Background: Human serum albumin (HSA) is one of the most abundant proteins in the blood plasma, urine as well as in the organic matrix of renal calculi. Macromolecules present in the urine modulate kidney stone formation either by stimulating or inhibiting crystallization process. Objective: In the present study, effect of HSA protein on the growth of calcium oxalate monohydrate crystal (COM) was investigated. Methods: Crystal growth assay was used to measure oxalate depletion in the crystal seeded solution in the presence of HSA. HSA concentrations exhibiting effect on crystal growth were selected for FTIR and XRD analysis. In silico docking was performed on seven different binding sites of HSA. Results: Albumin is playing dual role in growth of calcium oxalate crystallization. FTIR and XRD studies further revealed HSA exerted strain over crystal thus affecting its structure by interacting with amino acids of its pocket 1. Docking results indicate that out of 7 binding pocket in protein, calcium oxalate interacts with Arg-186 and Lys-190 amino acids of pocket 1. Conclusion: Our study confirms the role of HSA in calcium oxalate crystallization where acidic amino acids arginine and lysine are binding with COM crystals, revealing molecular interaction of macromolecule and crystal in urolithiasis.



2020 ◽  
Vol 54 (3 (253)) ◽  
pp. 261-264
Author(s):  
M.A. Shahinyan ◽  
N.H. Petrosyan ◽  
A.P. Antonyan

The interaction of methyl violet (MV) with human serum albumin (HSA) has been studied, using the fluorescence spectroscopy method. It was shown that MV chnages the own fluorescence of HSA. It was also shown that MV does not induce any conformational change in the structure of HSA, since there is no change of the wavelength of HSA fluorescence intensity maximum. MV binds to HSA, near to fluorescing tryptophan, which in the hydrophilic environment, and changes the own fluorescence of the protein.



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