详细信息
PEGDA hydrogel microspheres with encapsulated salt for versatile control of protein crystallization ( SCI-EXPANDED收录 EI收录)
文献类型:期刊文献
英文题名:PEGDA hydrogel microspheres with encapsulated salt for versatile control of protein crystallization
作者:Yan, Yizhen[1,2];Vladisavljevic, Goran T.[2];Lin, Zhichun[2];Yang, Huaiyu[2];Zhang, Xiangyang[1];Yuan, Weikang[1]
机构:[1]East China Univ Sci & Technol, State Key Lab Chem Engn, Shanghai 200237, Peoples R China;[2]Loughborough Univ, Dept Chem Engn, Loughborough LE11 3TU, Leics, England
年份:2024
卷号:660
起止页码:574
外文期刊名:JOURNAL OF COLLOID AND INTERFACE SCIENCE
收录:;EI(收录号:20240515477038);WOS:【SCI-EXPANDED(收录号:WOS:001174101900001)】;
基金:Xiangyang Zhang is grateful to the NSFC (National Natural Science Foundation of China) for support (No. 22078093) . Dr. Goran T. Vladisavljevic acknowledges the funding from Enterprise Project Group (EPG) , grant 18/14606 for the Lego-inspired device.
语种:英文
外文关键词:Hydrogel microsphere; Protein crystallization; Salt diffusion; Protein adsorption; Lysozyme
摘要:Due to their biocompatibility and adjustable chemical structure and morphology, hydrogels have great potential in many applications, and can be used to enhance protein crystal quality and crystallization efficiency, contributing to biomedicine manufacturing. Monodispersed PEGDA hydrogel microspheres (HMSs) were synthesized using a Lego-inspired microfluidic device. The generated droplets were then UV polymerized, partially hydrolyzed with 0.1 M NaOH solution to improve their absorption capacity, and soaked in a buffer solution containing 0, 0.5, 1, 2, and 4 M NaCl. Salt-loaded HMSs were used as the medium for the enhanced crystallization of hen egg white lysozyme from aqueous solutions. Different supersaturations were achieved in the protein solutions by releasing NaCl of different concentrations from HMSs, as confirmed by electrical conductivity measurements. HMSs with or without NaCl can both provide heterogeneous nucleation sites due to their nano-porous structure and wrinkled surface. The addition of NaCl-loaded HMSs to the protein solution can also increase or decrease the supersaturation in the whole solution or locally near the HMS, leading to controllable nucleation time and crystal size distribution dependent on the NaCl concentration loaded into HMSs.
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