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Probing the molecular interactions between cholinium-based ionic liquids and insulin aspart: A combined computational
Vidya Sundaram1, Ramakrishnan Nagasundara Ramanan2, Manikandan Selvaraj3
1Chemical Engineering Department, School of Engineering, Monash University Malaysia, Jalan Lagoon Selatan, 47500 Bandar Sunway, Selangor, Malaysia.
Cholinium-based ionic liquids (ILs) stabilize insulin aspart (IA), with dihydrogen phosphate ([Dhp]-) showing stronger effects than acetate ([Ace]-). IL concentration is key to maintaining IA stability against water molecules.
Area of Science:
- Biochemistry
- Physical Chemistry
- Materials Science
Background:
- Cholinium-based ionic liquids (ILs) show promise for protein stabilization.
- The specific interactions between IL components and protein residues remain unclear.
Purpose of the Study:
- Investigate the structural stability of insulin aspart (IA) in cholinium-based ILs.
- Elucidate the role of choline cation ([Ch]+) and anions ([Dhp]- or [Ace]-) in protein stabilization.
Main Methods:
- Combined computational (molecular docking) and experimental (spectroscopy, dynamic light scattering) approaches.
- Studied IA stability in 1 M [Ch][Dhp] and 1 M [Ch][Ace] solutions.
Main Results:
- IA remained structurally stable in both ILs, with [Dhp]- providing superior stabilization over [Ace]-.
- [Dhp]- and [Ace]- enhanced IA hydration but preserved the hydrophobic core.
- IL concentration was crucial for counteracting water's denaturing effects.
- Anions were found to have a dominant influence on IA structure, followed by the [Ch]+ cation.
Conclusions:
- Cholinium-based ILs, particularly those with [Dhp]-, can effectively stabilize insulin aspart.
- Understanding IL-protein interactions, especially the role of anions and IL concentration, is vital for protein stabilization applications.
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