Aqueous colloidal systems of bovine serum albumin and functionalized surface active ionic liquids for material transport

Singh, Gagandeep; Kaur, Manvir; Aswal, Vinod K.; Kang, Tejwant Singh

doi:10.1039/c9ra05549e

Cited by 17 publications

(13 citation statements)

References 66 publications

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“…An increase in the alkyl chain length of imidazolium cation of ILs hinders the fibrillation, which is well supported by the dissolution of fibrils of bovine serum albumin (BSA) and human serum albumin (HSA) by imidazolium-based surface-active ionic liquids (SAILs) to another aggregated morphologies. Such aggregated structures of BSA and other proteins in the presence of SAILs have also been reported by our group − with the exception of formation of long right-handedly twisted helical amyloid fibrils of BSA in aqueous solutions of ester-functionalized SAIL . This is contrary to the report by Kalhor et al, which is obvious considering the nature of the SAIL or IL used that would affect the nature and extent of interactions between two components.…”

Section: Introductioncontrasting

confidence: 51%

Spontaneous Fibrillation of Bovine Serum Albumin at Physiological Temperatures Promoted by Hydrolysis-Prone Ionic Liquids

et al. 2021

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This study highlights the role of time-dependent hydrolysis of ionic liquid anion, [BF4]−, of ionic liquid (IL), 1-ethyl-3-methylimidazolium tetrafluoroborate, [C2mim][BF4], which results in ever-changing pH conditions. Such pH changes along with the ionic interactions bring conformational changes in bovine serum albumin (BSA), leading to the formation of amyloid fibers at 37 °C without external control of pH or addition of electrolyte. The fibrillation of BSA occurs spontaneously with the addition of IL; however, the highest growth rate has been observed in aqueous solution of 10% IL (v/v %) among investigated systems. Thioflavin T (ThT) fluorescence emission has been employed to monitor the growth and development of β-sheet content in amyloid fibrils. The structural alterations in BSA have also been investigated using intrinsic fluorescence measurements. Circular dichroism (CD) measurements confirmed the formation of amyloid fibrils. Transmission electron microscopy (TEM) has been explored to establish the morphologies of BSA fibrils at different intervals of time, whereas atomic force microscopy (AFM) has established the helically twisted nature of grown amyloid fibrils. The docking studies have been utilized to understand the insertion of IL ions in different domains of BSA, which along with decreased pH cause the unfolding and growth of BSA into amyloid fibrils. It is expected that the results obtained from this study would help to understand the impact of IL containing [BF4]− anion on protein stability and aggregation along with providing a new platform to control the formation of amyloid fibrils and other biomaterials driven via ionic interactions and alterations in pH.

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Section: Introductioncontrasting

confidence: 51%

Spontaneous Fibrillation of Bovine Serum Albumin at Physiological Temperatures Promoted by Hydrolysis-Prone Ionic Liquids

et al. 2021

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“…However, the nature of the anion conjugated with the bio-ion (choline/amino acid as cation or anion) was found to strongly affect the IL toxicity 34,44 and their biophysical interaction with different enzymes/proteins. [45][46][47][48] Therefore, it is recommended to explore bio-derived alternatives for both cations and anions to design bio-ILs with desired chemical properties.…”

Section: Cytotoxicity Evaluation Of Gbilsmentioning

confidence: 99%

Good's buffer based highly biocompatible ionic liquid modified PLGA nanoparticles for the selective uptake in cancer cells

Singh,

Dasanayake,

Chism

et al. 2023

Mater. Chem. Front.

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“…This means that HSA molecules tend to maintain their folded structure and are less likely to denature or aggregate in solution, resulting in a more rigid and ordered solution structure. However, despite its higher conformational stability, HSA has been found to have lower colloidal stability than BSA [53]. This means that HSA molecules are more prone to aggregating or sticking together in solution, which can lead to a loss in stability and an increase in solution viscosity.…”

Section: Brillouin Scattering Of Bsa and Hsa Solutionsmentioning

confidence: 99%

Mechano-Chemistry across Phase Transitions in Heated Albumin Protein Solutions

et al. 2023

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The presence of certain proteins in biofluids such as synovial fluid, blood plasma, and saliva gives these fluids non-Newtonian viscoelastic properties. The amount of these protein macromolecules in biofluids is an important biomarker for the diagnosis of various health conditions, including Alzheimer’s disease, cardiovascular disorders, and joint quality. However, existing technologies for measuring the behavior of macromolecules in biofluids have limitations, such as long turnaround times, complex protocols, and insufficient sensitivity. To address these issues, we propose non-contact, optical Brillouin and Raman spectroscopy to assess the viscoelasticity and chemistry of non-Newtonian solutions, respectively, at different temperatures in several minutes. In this work, bovine and human serum albumin solution-based biopolymers were studied to obtain both their collective dynamics and molecular chemical evolution across heat-driven phase transitions at various protein concentrations. The observed phase transitions at elevated temperatures could be fully delayed in heated biopolymers by appropriately raising the level of protein concentration. The non-contact optical monitoring of viscoelastic and chemical property evolution could represent novel potential mechano-chemical biomarkers for disease diagnosis and subsequent treatment applications, including hyperthermia.

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Aqueous colloidal systems of bovine serum albumin and functionalized surface active ionic liquids for material transport

Abstract: Physicochemical and computational investigation of complexation between BSA and SAILs with application in material transport.

Cited by 17 publications

References 66 publications

Spontaneous Fibrillation of Bovine Serum Albumin at Physiological Temperatures Promoted by Hydrolysis-Prone Ionic Liquids

Spontaneous Fibrillation of Bovine Serum Albumin at Physiological Temperatures Promoted by Hydrolysis-Prone Ionic Liquids

Good's buffer based highly biocompatible ionic liquid modified PLGA nanoparticles for the selective uptake in cancer cells

Mechano-Chemistry across Phase Transitions in Heated Albumin Protein Solutions

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