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Polymerization-induced proteinosome formation
Journal of Materials Chemistry B ( IF 6.1 ) Pub Date : 2020-12-31 , DOI: 10.1039/d0tb02635b
Fang Liu 1, 2, 3, 4 , Yaqian Cai 1, 2, 3, 4 , Huan Wang 1, 2, 3, 4 , Xinlin Yang 1, 2, 3, 4 , Hanying Zhao 1, 2, 3, 4
Affiliation  

In recent years, the fabrication of well-organized proteinosomes has been a popular topic due to the potential applications of the structures in materials science and nanotechnology. A big challenge in the fabrication of proteinosomes is to maintain the structures and the functionalities of proteins on the proteinosomes. In this research, a new concept of polymerization-induced formation of proteinosomes is proposed. In thermal dispersion polymerization of N-isopropyl acrylamide (NIPAM) in the presence of bovine serum albumin (BSA), the growing PNIPAM chains experience phase transition from hydrated coils to dehydrated globules, and the dehydrated PNIPAM chains have hydrophobic interaction with BSA, leading to the formation of hollow proteinosomes. Kinetics studies indicate that there is a transition from the homogeneous polymerization of NIPAM in solution to the heterogeneous polymerization in the proteinosomes. Transmission electron microscopy, atomic force microscopy, confocal laser scanning microscopy and dynamic light scattering all demonstrate the formation of hollow structures. The results of circular dichroism spectroscopy indicate that the secondary structure of BSA remains unchanged in the polymerization process. The formation of proteinosomes is reversible. Upon cooling of the solution to a temperature below the phase transition temperature of PNIPAM, the proteinosomes are dissociated due to the absence of the hydrophobic interaction. The proteinosomes can be used in the encapsulation of hydrophilic compounds in aqueous solution. In this research, not only BSA but also ovalbumin (OVA) is used as a model protein for the fabrication of proteinosomes by the polymerization-induced approach.

中文翻译:

聚合诱导的蛋白体形成

近年来,由于结构在材料科学和纳米技术中的潜在应用,组织良好的蛋白质体的制造已成为热门话题。蛋白质体制造中的一大挑战是维持蛋白质体上蛋白质的结构和功能。在这项研究中,提出了聚合诱导蛋白质体形成的新概念。N的热分散聚合-异丙基丙烯酰胺(NIPAM)在牛血清白蛋白(BSA)的存在下,正在生长的PNIPAM链经历了从水合卷曲到脱水小球的相变,并且脱水PNIPAM链与BSA具有疏水相互作用,从而导致形成空心蛋白体。动力学研究表明,从溶液中NIPAM的均相聚合到蛋白体中的非均相聚合存在过渡。透射电子显微镜,原子力显微镜,共聚焦激光扫描显微镜和动态光散射都证明了中空结构的形成。圆二色性光谱的结果表明,BSA的二级结构在聚合过程中保持不变。蛋白体的形成是可逆的。在将溶液冷却至低于PNIPAM的相变温度的温度时,由于不存在疏水相互作用,使蛋白质体解离。蛋白质体可用于亲水性化合物在水溶液中的包封。在这项研究中,不仅BSA,而且卵白蛋白(OVA)都被用作通过聚合诱导方法制造蛋白体的模型蛋白。
更新日期:2021-01-19
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