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Thermosensitive polymer coated nanomagnetic particles for separation of bio-molecules

机译:用于分离生物分子的热敏聚合物包覆的纳米磁性颗粒

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Core-shell type thermosensitive magnetic particles were prepared via seed polymerization process.Double layer surfactant coated magnetic particles were first synthesized and then a rich poly-(iV-isopropylaciylamide)(PNIPAM)shell layer was attached using double layer magnetic particles as the seeds.Thiodiglycolic acid was used as the primary surfactant and 4-vinylaniline as the secondary surfactant.Carboxylated thermosensitive microspheres were prepared by adding methacrylic acid(MAA)in the polymerization process.PNIPAM has a lower critical solution temperature(LCST)of 32 °C in water,and changes from hydrophilic below the LCST to hydrophobic above it.The size of these thermosensitive polymer coated magnetic particles was measured by using transmission electron microscopy(TEM).TEM results show that magnetic particles were nanosized and the calculated mean diameter of the particles was about 12 nm.Bovine serum albumin(BSA)was selected as a model protein for the separation study.Adsorption of BSA on the thermosensitive magnetic particles was mainly dependent on the properties of the particles' surface.By increasing the temperature above the LCST of PNIPAM,the particles shrank and were able to adsorb larger quantity of proteins,which was subsequently desorbed at lower temperature.It was believed that carboxylated thermosensitive particles adsorb proteins through hydrogen bonding.When the two extremes of hydrophobic interaction and hydrogen bonding were compared,it was found that more proteins are adsorbed using the later interaction.
机译:通过种子聚合制备核-壳型热敏磁性粒子,首先合成双层表面活性剂包覆的磁性粒子,然后以双层磁性粒子为种子,附着丰富的聚(N-异丙基异丙基酰胺基)(PNIPAM)壳层。以巯基乙醇酸为主要表面活性剂,以4-乙烯基苯胺为辅助表面活性剂,通过在聚合过程中加入甲基丙烯酸(MAA)制备出羧基化的热敏微球,PNIPAM在水中的临界溶液温度(LCST)较低,为32°C。通过透射电子显微镜(TEM)测量了这些热敏性聚合物包覆的磁性粒子的尺寸。TEM结果表明,磁性粒子是纳米尺寸的,计算出的平均直径为大约12 nm处。选择牛血清白蛋白(BSA)作为模型蛋白进行分离研究。 BSA对热敏磁性颗粒的吸附主要取决于颗粒表面的性质。通过将温度提高到PNIPAM的LCST以上,颗粒会收缩并能够吸附大量蛋白质,随后在较低的温度下解吸。认为羧化的热敏颗粒通过氢键吸附蛋白质。当比较疏水相互作用和氢键这两个极端时,发现更多的蛋白质被后来的相互作用吸附。

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