Enhanced structural stability of insulin aspart in cholinium aminoate ionic liquids

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dc.contributor.author Sundaram, Vidya
dc.contributor.author Ramanan, Ramakrishnan Nagasundara
dc.contributor.author Selvaraj, Manikandan
dc.contributor.author Vijayaraghavan, R.
dc.contributor.author MacFarlane, Douglas R.
dc.contributor.author Ooi, Chien Wei
dc.coverage.spatial United States of America
dc.date.accessioned 2022-04-19T06:30:51Z
dc.date.available 2022-04-19T06:30:51Z
dc.date.issued 2022-03
dc.identifier.citation Sundaram, Vidya; Ramanan, Ramakrishnan Nagasundara; Selvaraj, Manikandan; Vijayaraghavan, R.; MacFarlane, Douglas R. and Ooi, Chien Wei, "Enhanced structural stability of insulin aspart in cholinium aminoate ionic liquids", International Journal of Biological Macromolecules, DOI: 10.1016/j.ijbiomac.2022.03.100, vol. 208, pp. 544-552, May 2022. en_US
dc.identifier.issn 0141-8130
dc.identifier.uri https://doi.org/10.1016/j.ijbiomac.2022.03.100
dc.identifier.uri https://repository.iitgn.ac.in/handle/123456789/7663
dc.description.abstract Cholinium aminoates [Ch][AA] have gained tremendous interest as a promising ionic liquid medium for the synthesis and storage of proteins. However, high alkalinity of [Ch][AA] limits its usage with pH-sensitive proteins. Here, we probed the structure, stability, and interactions of a highly unstable therapeutic protein, insulin aspart (IA), in a range of buffered [Ch][AA] (b-[Ch][AA]) using a combination of biophysical tools and in silico pipeline including ultraviolet-visible, fluorescence, and circular dichroism spectroscopies, dynamic light scattering measurements and molecular docking. b-[Ch][AA] used in the study differed in concentrations and their anionic counterparts. We reveal information on ion and residue specific solvent-protein interactions, demonstrating that the structural stability of IA was enhanced by a buffered cholinium prolinate. In comparison to the glycinate and alaninate anions, the hydrophilic prolinate anions established more hydrogen bonds with the residues of IA and provided a less polar environment that favours the preservation of IA in its active monomeric form, opening new opportunities for utilizing [Ch][AA] as storage medium.
dc.description.statementofresponsibility by Vidya Sundaram, Ramakrishnan Nagasundara Ramanan, Manikandan Selvaraj, R. Vijayaraghavan, Douglas R. MacFarlane and Chien Wei Ooi
dc.format.extent vol. 208, pp. 544-552
dc.language.iso en_US en_US
dc.publisher Elsevier en_US
dc.subject Cholinium aminoates en_US
dc.subject Ionic liquids en_US
dc.subject Insulin aspart en_US
dc.subject Protein stabilization en_US
dc.subject Protein-IL interaction en_US
dc.title Enhanced structural stability of insulin aspart in cholinium aminoate ionic liquids en_US
dc.type Article en_US
dc.relation.journal International Journal of Biological Macromolecules


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