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

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.

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STUDY OF ABSORPTION SPECTRA OF THE COMPLEXES OF BOVINE SERUM ALBUMIN WITH HOECHST 33258 AND METHYLENE BLUE

Proceedings of the YSU B: Chemical and Biological Sciences ◽

10.46991/pysu:b/2021.55.2.158 ◽

2021 ◽

Vol 55 (2 (255)) ◽

pp. 158-164

Author(s):

Nara H. Petrosyan

Keyword(s):

Methylene Blue ◽

Serum Albumin ◽

Absorption Spectra ◽

Hoechst 33258 ◽

Differential Absorption ◽

Partial Loss ◽

Groove Binding ◽

Compact Structure ◽

Binding Material ◽

Molecular Compounds

The study on the interaction of DNA-specific low-molecular compounds – groove binding material Hoechst 33258 and intercalating ligand methylene blue (MB) with serum albumin has been carried out. The absorption and differential absorption spectra of complexes of the mentioned ligands with protein were obtained. Changes of the absorption and differential absorption spectra indicate the binding of two ligands with albumin. The obtained results indicate that at the interaction with both ligands, the conformational state of the protein alters, though these changes are not similar, since in the case of MB a compactization of the protein folding occurs, while in the case of Hoechst 33258, most apparently, an unfolding of the compact structure takes place as a result of partial loss of helicity of $\alpha$-structures.

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

Proceedings of the YSU B: Chemical and Biological Sciences ◽

10.46991/pysu:b/2020.54.3.204 ◽

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.

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