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

Authors

  • P.O. Vardevanyan Chair of Biophysics, YSU, Armenia
  • M.S. Mikaelyan Chair of Biophysics, YSU, Armenia
  • N.H. Petrosyan Armenia Diagen Plus LLC, Armenia

DOI:

https://doi.org/10.46991/PYSU:B/2020.54.3.204

Keywords:

bovine serum albumin, methylene blue, Hoechst 33258, interaction, denaturation temperature

Abstract

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.

Downloads

Published

2020-12-15

How to Cite

Vardevanyan, P.O., M.S. Mikaelyan, and N.H. Petrosyan. 2020. “BOVINE SERUM ALBUMIN DENATURATION IN THE PRESENCE OF HOECHST 33258 AND METHYLENE BLUE”. Proceedings of the YSU B: Chemical and Biological Sciences 54 (3 (253):204-8. https://doi.org/10.46991/PYSU:B/2020.54.3.204.

Issue

Vol. 54 No. 3 (253) (2020)

Section

Biology

License

Copyright (c) 2020 Proceedings of the YSU

Creative Commons License

This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

Most read articles by the same author(s)