Li Fu, Xiaoxia Peng, Yaxue Shen, Zhuojia Shi, Ziying Zhen, Ran Sun, Yaqi Wu, Liu Lu, Yu Chen
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引用次数: 0
Abstract
Thermodynamics and interaction between human serum albumin (HSA) and low-melting mixture solvents (LoMMSs) play a critical role in the green and low-cost separation of proteins. To the best of our knowledge, there have been no reports on this issue to date. Here, we present the thermodynamic properties and single-site interaction between biobased LoMMSs betaine:glycerol and HSA. LoMMSs demonstrate strong binding affinity toward HSA, driven primarily by van der Waals forces and hydrogen bonding. LoMMSs can stabilize the secondary structure of HSA, preserving its functional integrity. This work provides valuable insights to design green, sustainable, and cost-effective LoMMSs for protein purification.
期刊介绍:
Biomacromolecules is a leading forum for the dissemination of cutting-edge research at the interface of polymer science and biology. Submissions to Biomacromolecules should contain strong elements of innovation in terms of macromolecular design, synthesis and characterization, or in the application of polymer materials to biology and medicine.
Topics covered by Biomacromolecules include, but are not exclusively limited to: sustainable polymers, polymers based on natural and renewable resources, degradable polymers, polymer conjugates, polymeric drugs, polymers in biocatalysis, biomacromolecular assembly, biomimetic polymers, polymer-biomineral hybrids, biomimetic-polymer processing, polymer recycling, bioactive polymer surfaces, original polymer design for biomedical applications such as immunotherapy, drug delivery, gene delivery, antimicrobial applications, diagnostic imaging and biosensing, polymers in tissue engineering and regenerative medicine, polymeric scaffolds and hydrogels for cell culture and delivery.