Study of Thermal Denaturing of Human Serum Albumin in the Presence of Potassium Chloride by the Excitation/Emission Matrix Method

Grigoryan, K. R.; Shilajyan, Hasmik A.

doi:10.1007/s10812-013-9844-y

Cited by 6 publications

(2 citation statements)

References 7 publications

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“…The d H for BSA and HSA at 25 °C in a buffer (pH 7) was found to be ∼7.9 and ∼7.8 nm, respectively. These data matches well with already reported data. − It was observed that in the presence of a varying concentration of ILs, no significant changes accompanied the native BSA structure as indicated in Figures 7S and 8S. Furthermore, with the introduction of urea in BSA, the d H has increased dramatically as indicated in Figures 7Sa and 8Sa.…”

Section: Resultssupporting

confidence: 91%

“…The T m values of BSA in a buffer, ILs, and IL + urea are illustrated in Figure a,b as well as Tables 1S and 2S (Supporting Information). The T m of native BSA in buffer was found to be 55.1 °C, which correlates well with the available literature. , The thermal stability of BSA is enhanced in the presence of both the ILs as evident from Figure a,b. Thus, the proposed ILs are stabilizing the native BSA structure against temperature effect.…”

Section: Resultssupporting

confidence: 89%

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Implications of Imidazolium-Based Ionic Liquids as Refolding Additives for Urea-Induced Denatured Serum Albumins

Sindhu

Bhakuni

Sankaranarayanan

et al. 2019

ACS Sustainable Chem. Eng.

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One of the major challenges in protein stability is that proteins can easily unfold in the presence of denaturants like urea, which alters the native structure of proteins. There are numerous studies in which ionic liquids (ILs) act as promising biocompatible solvents (Bio-IL) for biomolecules. In this context, we present the refolding ability of biocompatible imidazolium-based ILs, 1-ethyl 3-methyl imidazolium ethyl sulfate [Emim][ESO4] (IL-1) and 1-ethyl 3-methyl imidazolium chloride [Emim][Cl] (IL-2) against the chemically induced structural changes in bovine and human serum albumin (BSA and HSA). The work is substantiated with several spectroscopic, thermal and docking studies. In steady-state fluorescence spectroscopy, we observe that the emission intensity quenches for the protein in urea, which is reversible with the addition of ILs. Circular dichroism spectral studies reflect the reappearance of α helical content, which is a good indicator of the refolding ability of ILs. Further, thermal fluorescence studies showed that ILs have the ability to refold the urea-induced denatured protein at a higher temperature range only up to 7 M urea concentration; however, above 7 M urea concentration, IL somehow fails to refold the protein. The work is also supported by dynamic light scattering measurements, and the degree of BSA/HSA aggregation was reduced with the introduction of Bio-IL to the urea–BSA/urea–HSA system, ensuring the aggregate-free refolding. Furthermore, molecular docking studies were employed to probe the binding sites, and the results are well corroborated with the spectroscopic and thermal folding results. Therefore, through this paper, we aim to unravel the mechanistic intricacy of ILs using experimental and docking approaches. Overall, ILs act as recoiling medium for both native and unfolded (denatured by urea) BSA/HSA native structures.

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Section: Resultssupporting

confidence: 91%

Section: Resultssupporting

confidence: 89%