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作 者:Chi Li Jia-Ning Zhang Jing Jin Wei Jiang
机构地区:[1]State Key Laboratory of Polymer Physics and Chemistry,Changchun Institute of Applied Chemistry,Chinese Academy of Sciences,Changchun 130022,China [2]School of Applied Chemistry and Engineering,University of Science and Technology of China,Hefei 230026,China
出 处:《Chinese Journal of Polymer Science》2023年第12期1879-1888,I0007,共11页高分子科学(英文版)
基 金:financially supported by the National Natural Science Foundation of China(No.52073276);Changchun Science and Technology Development Program(No.21ZY07);the Innovation and Entrepreneurship Talent Project of Jilin Province.
摘 要:PEGylation is the gold standard for constructing protein resistance surfaces.Herein,grafting mPEG-SH and SH-PEG-SH with varied molecular weights(Mw=5K,10K,and 20K)on a gold chip,and the subsequent lysozyme adsorptions of the PEG layers are evaluated using quartzcrystal microbalance based on dissipation(QCM-D).The lysozyme resistance depends on the features of grafting density and chain conformation,i.e.,linear and looped conformation.However,long-chain PEG(Mw≥10K)is insufficient to form a dense layer to resist protein due to large steric hindrances.Short-chain PEG(Mw=1K)with linear and looped structures is used to refill onto the long-chain PEG layer to increase the grafting density of PEGs and improve protein resistance.The refilling process and the subsequent protein adsorption depend on conformation rather than the density of the long-chain PEG substrate.Notably,the long-chain PEG looped substrates significantly improve protein resistance,attributing to the high viscoelasticity of the looped substrate and an increase in grafting density after refilling.Thus,refilling short-chain PEG improves protein resistance and the substrate conformation-dependence gives insight into the impact of topology,providing new ideas for how to increase chain density and select suitable topology to resist protein adsorption and demonstrating a potential application in biomedical fields.
关 键 词:Poly(ethylene glycol) REFILLING Protein adsorption CONFORMATION QCM-D
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