Search
Organic solvents aggregating and shaping structural folding of protein, a case study of the protease enzyme
Abstract
Low solubility of reactants or products in aqueous solutions can result in the enzymatic catalytic reactions that can occur in non-aqueous solutions. In current study we investigated aqueous solutions containing different organic solvents / deep eutectic solvents (DESs) that can influence the protease enzyme's activity, structural, and thermal stabilities. Retroviral aspartic protease enzyme is responsible for the cleavage of the polypeptide pre- cursors into mature viral components, a very crucial step for virus life cycle. In molecular dynamic simulations (MDS), the complex of the protease enzyme with Darunavirwas found highly stable in urea aqueous solution compared to when with the ethylene glycol (EG) or glycerol solvents. Particularly, in different organic solvents the presence of Darunavir induced protein-protein interactions within the protease homodimer. For the systems with EG or glycerol solvents, the flap domains of the enzyme formed an “open” conformation which lead to a weak binding affinity with the drug. Conserved D25 and G27 residues among this family of the aspartic protease enzymes made a stable binding with Darunavir in the urea systems. Unfolding of the protease dimer was initiated due to self-aggregation for the EG or glycerol organic solvents, which formed an “open” conformation for the flap domains. On the contrary lack of such clustering in urea solvent, the protease showed conventional structural folding in the presence or absence of the drug molecule. These novel findings may help to better understand the protease enzymes, which could be controlled by deep eutectic solvents.
Citations
-
2
CrossRef
-
0
Web of Science
-
3
Scopus
Authors (4)
-
Monikaben Padariya
-
Minofar Babak
Cite as
Full text
- Publication version
- Accepted or Published Version
- DOI:
- Digital Object Identifier (open in new tab) 10.1016/j.bpc.2022.106909
- License
-
open in new tab
Keywords
Details
- Category:
- Articles
- Type:
- artykuły w czasopismach
- Published in:
-
BIOPHYSICAL CHEMISTRY
no. 291,
ISSN: 0301-4622 - Language:
- English
- Publication year:
- 2022
- Bibliographic description:
- Padariya M., Bagiński M., Babak M., Kalathiya U.: Organic solvents aggregating and shaping structural folding of protein, a case study of the protease enzyme// BIOPHYSICAL CHEMISTRY -Vol. 291, (2022), s.106909-
- DOI:
- Digital Object Identifier (open in new tab) 10.1016/j.bpc.2022.106909
- Sources of funding:
-
- Projekt zewnętrzny UG: The International Centre for Cancer Vaccine Science (Fundacja na rzecz Nauki Polskiej MAB/3/2017
- Verified by:
- Gdańsk University of Technology
seen 86 times
Recommended for you
Deep Eutectic Solvents as Agents for Improving the Solubility of Edaravone: Experimental and Theoretical Considerations
- T. Jeliński,
- M. Przybyłek,
- M. Mianowana
- + 2 authors
Deep Eutectic Solvents as Agents for Improving the Solubility of Edaravone: Experimental and Theoretical Considerations
- T. Jeliński,
- M. Przybyłek,
- M. Mianowana
- + 2 authors