BOVINE SERUM ALBUMIN DENATURATION IN THE PRESENCE OF HOECHST 33258 AND METHYLENE BLUE

2020 ◽  
Vol 54 (3 (253)) ◽  
pp. 204-208
Author(s):  
P.O. Vardevanyan ◽  
M.S. Mikaelyan ◽  
N.H. Petrosyan
Keyword(s):  
Methylene Blue ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Denaturation ◽  
Native Structure ◽  
Hoechst 33258 ◽  
Denaturation Temperature

The interaction of Hoechst 33258 (H33258) and methylene blue (MB) compounds with bovine serum albumin (BSA) has been studied using the method of thermal denaturation. The obtained data showed that both ligands form complexes with BSA, moreover, MB binds to BSA stronger than H33258. Furthermore, H33258 destabilizes, while MB stabilizes the native structure of protein, leading to the decrease and increase of the denaturation temperature of BSA respectively.

COMPARATIVE STUDY OF SPECTRAL CHARACTERISTICS OF COMPLEXES OF HOECHST 33258 AND METHYLENE BLUE WITH BOVINE SERUM ALBUMIN

2021 ◽  
Vol 88 (6) ◽  
pp. 942-947
Author(s):  
A. P. Antonyan ◽  
N. H. Petrosyan ◽  
P. O. Vardevanyan
Keyword(s):  
Methylene Blue ◽  
Bovine Serum Albumin ◽  
Comparative Study ◽  
Serum Albumin ◽  
Absorption Spectra ◽  
Bovine Serum ◽  
Hoechst 33258 ◽  
Differential Absorption ◽  
Denaturation Temperature ◽  
Compact Structure

The comparative study on interaction of bisbenzimidazole compound Hoechst 33258 and thiazine dye methylene blue (MB) with bovine serum albumin (BSA) was carried out by spectroscopic methods. Denaturation curves as well as absorption spectra and differential absorption spectra of protein-ligand complexes were obtained. Denaturation temperature of albumin complexes of BSA with Hoechst 33258 was shown to decrease with the growth of concentration ratio of ligand/protein, while for MB, vice versa, denaturation temperature increases. Changes in absorption spectra and differential absorption spectra of the complexes of ligands with albumin were revealed, which result from the binding of these DNA-specific ligands to protein. It is supposed that at the interaction of Hoechst 33258 with BSA some loosening of protein compact structure occurs due to the partial loss of helicity of α-structures, while for MB an increase of the protein compact structure takes place.

scholarly journals The Interaction of Methylene Blue and Bovine Serum Albumin in SDS Micelle System

2001 ◽  
Vol 17 (02) ◽  
pp. 185-188 ◽  
Author(s):  
Guo Rong ◽  
◽  
Fan Guo-Kang ◽  
Liu Tian-Qing ◽  
Jiao Xin-An
Keyword(s):  
Methylene Blue ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sds Micelle ◽  
Micelle System

Bovine serum albumin determination based on methylene blue detection by photothermal lens spectroscopy

2020 ◽  
Vol 594 ◽  
pp. 113621
Author(s):  
Behnaz Abbasgholi Nejad Asbaghi ◽  
Nader Shokoufi ◽  
Shafigh Nouri Hajibaba
Keyword(s):  
Methylene Blue ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

Thermal denaturation of bovine serum albumin and its oligomers and derivativespH dependence

1995 ◽  
Vol 45 (6) ◽  
pp. 1255-1264 ◽  
Author(s):  
G. Barone ◽  
S. Capasso ◽  
P. Del Vecchio ◽  
C. De Sena ◽  
D. Fessas ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Denaturation
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