Deep Eutectic Solvents: Properties and Protein Interaction [Part A]
BSA in Urea-Sarcosine DES: Solubility, Aggregation, and Storage Stability [Part B]
Publication Date
December 12, 2025
Creator
Abstract
Part A
In recent years, green solvents have emerged as an alternative to replace toxic organic solvents, deep eutectic solvents (DESs) is a new type of green solvents which have a great development prospect. They are mixtures of two compounds which have a lower melting point due to their unique physicochemical properties. This kind of new green solvents can be used in many fields because of their low toxicity and become more and more popular. Deep eutectic solvents are formed through hydrogen bonding between the hydrogen bond donor (HBD) and the hydrogen bond acceptor (HBA) and have more advantages than traditional ionic liquids and organic solvents. They have
many applications in drug delivery and protein extraction. The main physicochemical properties of them have been studied are phase behaviour, viscosity and density in this paper. Moreover, they can interact with protein through several mechanisms which are hydrogen bonds, hydrophobic interactions, salting out effects and electrostatic forces. These mechanisms influence the structure and function of proteins. Additionally, urea and sarcosine are also useful in DES system. In conclusion, DES is a new generation of green solvents and show a wide application prospect in the field of protein science.
Part B
This study investigated the effects of a urea-sarcosine deep eutectic solvents (DES, molar ratio 5:2) at different water contents (50% and 80%) on the solubility, aggregation behaviour, and storage stability of bovine serum albumin (BSA). Results demonstrated that this DES system formed a stable homogeneous liquid, with viscosity and density increasing as water content decreased, while pH remained neutral. At attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR) confirmed the formation of a strong hydrogen-bond network in the DES. BSA solubility in the DES increased with rising DES content. Dynamic light scattering (DLS) and analytical
ultracentrifugation sedimentation velocity (AUC-SV) revealed that DES effectively inhibited BSA aggregation, demonstrating excellent stability protection particularly under high-temperature (40°C). The 80% water content DES exhibited optimal anti-aggregation efficacy at elevated temperatures. AUC analysis further indicated that 80% water content DES promotes reversible self-association behaviour in BSA, whereas this phenomenon was not observed in 50% water content DES. This study confirms that urea-sarcosine DES is a green solvent which can enhance protein stability, demonstrating potential for application in biotechnology field.
Item Type
ethesis
Thesis Type
MRes
Supervisors
Subjects (LC)
Associated Schools / Departments
School of Biosciences (UK)
eprints ID
82735
UoN Repository URI
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