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- W4280591368 abstract "Background: Arginine deiminase enzyme of Mycoplasma arginini (MaADI) is a potential anti-cancer agent for treating arginine-auxotrophic cancers. Investigating the protein stability in the presence of osmolytes can help to increase protein stability under various stressed conditions. Methods: In this study, the stability and dynamics of MaADI were investigated in pure water and solutions of 1 M sorbitol, 10% (v/v) methanol, and 50% (v/v) methanol using molecular dynamics simulation. Results: Sorbitol was found to stabilize the protein, whereas high-concentrated methanol destabilized it. Sorbitol molecules interacted with the protein through hydrogen bonding and reduced the protein fluctuations as well. At 50% methanol, the flexibility of regions 4-8, 195-201, 314-324, and 332-337 in the MaADI was increased; whereas residues 195-201 showed the highest variations. Conclusion: Thus, these regions of MaADI, especially 195-201, are the most sensitive regions in the presence of denaturing agents and can be subjected to protein engineering toward improving the stability of MaADI." @default.
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- W4280591368 date "2022-10-01" @default.
- W4280591368 modified "2023-09-27" @default.
- W4280591368 title "Methanol and Sorbitol Affect the Molecular Dynamics of Arginine Deiminase: Insights for Improving its Stability" @default.
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- W4280591368 doi "https://doi.org/10.2174/1570164619666220513123509" @default.
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