氨基表面修饰的高分子乳液微球对牛血白质BSA吸附性能的研究

以苯乙烯St和甲基丙烯酸环氧丙酯GMA为单体,两性偶氮类化合物V50为引发剂,运用功能单体多段加料的无皂乳液聚合法制备亲和高分子乳液基球PSG,并选择双氨基封端的聚乙二醇作为空间臂分子,进行表面修饰反应,考察了高分子乳液微球对牛血蛋白BSA的吸附性能,并着重研究了吸附时间和温度、BSA初始浓度、离子强度等因素对吸附反应的影响。实验结果表明,空间臂表面修饰的高分子微球作为载体材料,固定药物分子等生物活性物质,可通过控制吸附条件,如pH,温度,反应时间等,减少蛋白质分子的非特异性吸附,且保持生化分子的较高活性。     

静电耦合亲和层析纯化人血清白蛋白的研究

人血清白蛋白(Human Serum Albumin,HSA)是人血清中含量最丰富的蛋白，约占血清总蛋白含量的40%～60%。商品化的白蛋白亲和介质(Cibacron Blue F3GA)的配基毒性大、易脱落、载量低，纯化白蛋白回收率较低。本研究制备了一种新型静电耦合亲和介质(DASA-Sepharose,3,5-Diaminobenzoic Acid n-Octyl Succinic Anhydride-Sepharose)，并通过一步层析从人血清中高效纯化白蛋白。DASA-Sepharose介质采用3,5-二氨基苯甲酸间隔臂将正辛基琥珀酸酐亲和配体偶联于琼脂糖微球。DASA-Sepharose间隔臂上的羧基通过静电作用吸附白蛋白，进而与正辛基琥珀酸酐亲和配基协同作用实现静电耦合亲和吸附，在保持亲和吸附高特异性的同时大大提高了吸附载量。采用牛血清白蛋白(Bovine Serum Albumin,BSA)为模型蛋白考察了Na Cl浓度和溶液pH对介质静态吸附载量(Q_m)的影响，NaCl浓度为0.025～0.06 mol/L时Q_m几乎不受影响，...     

高磁场响应性蛋白偶联磁性微球的制备及其在药物-蛋白结合常数测定中的应用

以蛋白偶联磁性微球(MB)为固相基质,通过磁场下快速分离蛋白和上清,高效液相色谱法测定上清中的药物浓度,建立了测定药物与蛋白结合常数(Ka)的新方法。选择对药物非特异性吸附较少和磁响应性较高的四氧化三铁磁性微球为载体,分别以1-(3-二甲氨基丙基)-3-乙基碳二亚胺盐酸盐/N-羟基琥珀酰亚胺(EDC/NHS)及戊二醛作为偶联剂,制备牛血清白蛋白(BSA)包覆的磁性微球(MB-BSA),两种偶联方法所得磁性微球的蛋白最大键合量均为50μg/mg。以布洛芬为模型药物,研究药物在蛋白偶联磁性微球上的吸附行为及药物-蛋白的相互作用模式,优化药物吸附和解吸过程。利用高效液相色谱法测定经磁性分离的上清液中的游离药物浓度,通过罗森塔尔方程计算药物与BSA结合常数。最后将所建立的方法应用到色氨酸、安立生坦、瑞替加滨、罗氟司特等4种不同药物与蛋白的结合常数的测定,获得满意结果。     

多孔聚(甲基丙烯酸环氧丙酯-二乙烯基苯)微球的改性及作为蛋白质疏水层析介质的应用

用悬浮聚合方法合成了富含环氧基团的多孔聚(甲基丙烯酸环氧丙酯-二乙烯基苯) [Poly(Glycidyl Methacrylate-Divinylbenzene), P(GMA-DVB)]微球,为了消除其对蛋白质的不可逆吸附,探索用聚乙二醇(Polyethylene Glycol, PEG)对微球进行改性,制备了带有PEG配基的P(GMA-DVB)微球. 实验考察了反应条件对PEG固载量的影响规律,发现最适反应温度为80℃. 以牛血清白蛋白(Bovine Serum Albumin, BSA)和胰蛋白酶作为模型蛋白,考察了PEG改性前后P(GMA-DVB)微球对蛋白质的吸附性能. 改性前P(GMA-DVB)微球有30%~40%的不可逆吸附,蛋白质回收率仅为60%~70%. 改性后介质消除了不可逆吸附,对蛋白质的吸附作用表现为可逆的疏水相互作用,吸附BSA和胰蛋白酶的质量回收率和活性回收率都在97%以上. 结果表明,PEG-P(GMA-DVB)微球可以作为一种新型介质进一步应用于蛋白质的吸附与分离.     

表面带磺酸基团的聚苯乙烯微球的制备及其对蛋白质的吸附

研究了运用分散聚合法,在乙醇/水混合介质中,制备2-丙烯酰胺基-2-甲基丙磺酸(AMPS)与苯乙烯(St)的共聚微球。运用红外、核磁共振、激光光散射和扫描电子显微镜对功能微球进行表征。阐述了该微球对牛血清蛋白(BSA)的吸附量与吸附时间和pH值的关系。结果表明:功能微球对BSA的吸附先随时间的增长而增大,一段时间后达到平衡吸附。当pH值接近BSA等电点(pI=4.7)时,BSA的吸附量达到最大值。     

一种新型的负载蛋白质药物微球的制备和释药性能

为了制备具有蛋白药物结肠靶向释放性能的新型药物载体,采用了水相溶液滴定反应法,分别以牛血清白蛋白(BSA)和乳铁蛋白(LF)为模型蛋白质药物,制得壳聚糖/纤维素磷酸钠(NaCS)/三聚磷酸钠(TPP)载药微球。利用电镜SEM和显微镜观测拍照,对微球的表面和截面形貌进行了表征,发现微球球形规则且颗粒大小均一。同时进行了体外药物模拟释放试验,考察了载药微球先后经过模拟胃液、模拟小肠液和模拟结肠液时的释药性能,及不同的释放条件和制造条件对于微球释药性能的影响,尤其考察了不同蛋白药物和不同干燥方式的影响。结果表明由临界点干燥法制得的负载乳铁蛋白(LF)微球在模拟胃液和小肠液释放量中5 h内只释放出不到20%的蛋白药物,而后在结肠模拟液中4 h内释放出蛋白药物80%以上。这些结果表明,壳聚糖/NaCS/TPP体系具有一定的作为结肠靶向药物释放载体的应用潜力。     

亲和高分子乳液微球研究进展

综述了亲和高分子乳液微球的结构组成、特点和应用,并概括了亲和高分子乳液微球的当今研究动态和发展前景.     

双乳化-凝胶法制备单分散海藻酸钙微球及其载BSA研究

采用双乳化-凝胶法制备了单分散的海藻酸钙凝胶微球,并通过正交试验系统考察了海藻酸钠浓度、氯化钙浓度、表面活性剂浓度、搅拌速度和油水比对海藻酸钙凝胶微球粒径及形貌的影响。在优化的条件下,制备出了平均粒径为4μm、单分散和球形度好的海藻酸钙凝胶微球。包埋模型药物牛血清白蛋白(BSA)的过程中,以去离子水作为洗涤液洗涤海藻酸钙微球时,BSA的包封率仅为13%左右;当水洗液的pH值为3.2时,BSA的包封率提高到66%左右,载药率可达16%,这是海藻酸钙pH值响应溶胀和BSA与海藻酸盐之间静电作用的结果。微球中BSA的体外释放曲线表明,该系统具有在模拟胃液中释药速率慢、释药量低、模拟肠液中释药迅速的特性。因此,双乳化-凝胶法制备海藻酸钙微球有望成为制备蛋白类药物控释制剂的一种新方法,以达到靶向快速给药的目的。     

磁性微球与蛋白质相互作用的微量热研究

以牛血清白蛋白(BSA)为生物模型,采用微量热法自动跟踪磁性微球与BSA相互作用的全过程,研究了磁性微球与BSA相互作用的微量热;采用分光光度法测定了磁性微球所吸附的蛋白质容量;建立了磁性微球表面性质与蛋白质吸附容量的关系.结果表明,微量热法与传统的光度法所得结果大致相当,即相互作用的热越多,吸附蛋白质的容量越大,而且偶联羧基的磁性微球比无官能团的微球具有更大的吸附热和吸附容量.     

磁性壳聚糖微球固定化小牛白蛋白的研究

考察了磁性壳聚糖微球对磷酸氢二钠-柠檬酸缓冲溶液中小牛白蛋白的吸附性能,采用TEM(透射电镜)、XRD(X-射线粉末衍射)分析微球的形貌、组成,深入探讨了磁性壳聚糖微球用量对蛋白质脱除率的影响、吸附温度和蛋白质溶液离子强度对微球吸附性能的影响。实验结果表明,蛋白质脱除率随磁性壳聚糖微球用量增大而增大,最终趋于平稳;随着温度升高,微球吸附蛋白量先增加后减小;蛋白溶液离子强度增加,微球吸附蛋白量降低。     

铅离子印迹聚合物微球的制备及其吸附性能研究

以Pb2+为模板,甲基丙烯酸(MAA)为功能单体,乙二醇二甲基丙烯酸酯(EDMA)为交联剂,十二烷基苯磺酸钠(SDBS)为分散剂,采用乳液悬浮聚合法制备了铅离子印迹聚合物微球。通过静态平衡吸附实验和Scatchard分析法研究了聚合物微球的吸附性能和选择性。结果表明,铅离子印迹聚合微球能有效去除溶液中的铅离子,最大吸附容量为15.29 mg/g。在竞争离子Cd2+存在的溶液中,铅离子印迹聚合物微球呈现出对铅离子的高选择性。Pb2+/Cd2+的识别因子为19.01,结合位点的离解常数Kd=35.61 mg/L,最大表观结合量Qmax=25.19 mg/g。     

Magnetic polymer microsphere with photoconductivity: preparation and characterization of iron(III) phthalocyanine covalently bonded on to polystyrene microsphere surface

A novel magnetic polymer microsphere displaying photoconductivity was prepared by covalently bonding iron(III) phthalocyanine (FePc) onto a polystyrene microsphere with hydroxyl groups (PSA). PSA was synthesized by dispersion polymerization in the presence of Fe₃O₄ magnetic fluid. The structure and properties of the magnetic polymer microsphere were identified by infrared spectoscopy. elemental analysis and scanning electron microscopy. The results showed that this kind of microsphere combines the merits of magnetic responsiveness and photoconductivity. The application of magnetic polymer microspheres for absorption of bovine serum albumin (BSA) was characterized at different temperatures, different incubation times, different pH values and different initial BSA concentrations. © 2002 Society of Chemical Industry     

累托石/腐殖酸微球对水中蒽的吸附

采用累托石、腐殖酸、聚乙烯醇、海藻酸钠和氯化钙等材料制备微球状吸附剂去除水中多环芳烃蒽。考察了微球用量、蒽溶液初始浓度、吸附时间等因素对吸附效果的影响,测定了吸附等温线,采用Freundlich、Langmuir模式对等温吸附规律作了数学模拟,对吸附动力学及吸附机理进行了探讨。结果表明:在该研究条件下,微球用量、溶液初始浓度、吸附时间等因素对水中蒽的吸附效果有显著性影响。最优吸附条件为:微球用量=5 g/50 mL,初始浓度=10 mg/L,吸附时间=14 h。累托石/腐殖酸微球对水中蒽的等温吸附规律符合Freundlich和Langmuir模型,吸附动力学过程可用准一级、准二级动力学模式和双常数方程较好地模拟。吸附是靠微球与蒽的分子间作用力来实现的。     

壳聚糖表面胰蛋白酶分子印迹聚合物的制备及性能的研究

在壳聚糖表面通过希夫碱反应嫁接一层戊二醛,形成核-壳结构微球。然后在这个核-壳微球上,以胰蛋白酶为模板分子,3-氨基苯硼酸为功能单体,制备了胰蛋白酶分子印迹聚合物,通过静态吸附法,研究了聚合物的吸附性能。结果表明,印迹聚合物对模板分子有较高吸附容量和特异选择性。为从蛋白质混和溶液中分离富集胰蛋白酶提供了新的材料和方法。     

Protein–polymer interaction: Transfer loading at interfacial region of PES-based membrane and BSA

The adsorption of proteins onto polymeric surfaces is encountered in many natural and industrial processes and is a prerequisite to their efficient identification, separation, and purification by methods such as chromatography, and filtration. Nevertheless, the exact nature of the adsorption mechanisms and interfacial interactions is not easy to identify for a given protein–polymer system. Here, we aim to document the adsorption mechanism of a protein–polymer system by investigating the adsorption as well as desorption phenomenon of a protein [bovine serum albumin (BSA)] from the polymeric surface [polyethersulfone (PES)]. The analyses performed to document the adsorption mechanism of the BSA–PES system include scanning electron microscope (SEM), attenuated total reflection-Fourier transform infrared (FTIR), contact angle, zeta potential, surface charge density measurement, and Derjaguin–Landau–Verwey–Overbeek (DLVO). Here, SEM and FTIR identified the physical and chemical properties of pure PES and PES–BSA membranes. The low water contact angle of the PES–BSA membrane confirms its applicability for tissue engineering applications. Further, the zeta potential, surface charge density measurement, and DLVO analyses were performed to document the adsorption mechanism. The adsorption of BSA particles on the PES surface was carried out for pH values that ranged from 4 to 10 for contact times that ranged from 1 to 3 days. A monotonic increase in the zeta potential of the PES–BSA system indicated considerable adsorption of BSA particles on the PES surface. Further, BSA adsorption was very strong for pH values greater than 4.7 which confirms to strong electrostatic interactions between BSA and PES. The strong electrostatic interaction is also collaborated by low desorption rate, which was only ∼22% for pH 10 after 3 days of contact. © 2019 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2019 , 136, 47931.     

Anti-nonspecific adsorption segments-assisted self-driven surface imprinted fibers for efficient protein separation

At present, the development of high-performance protein imprinted materials is still a research hotspot in the field of protein imprinting. Herein, anti-protein adsorption segment (CBMA)-assisted self-driven bovine serum albumin (BSA) surface imprinted fibers MTCFs@SIP@CBMA with high recognition selectivity are pioneered using the strategies of combining magnetic nanomaterial surface imprinting technique with amino-Michael addition. The special structure of the carrier MTCFs endows MTCFs@SIP@CBMA with magnetic performance and self-driven adsorption performance, which simplifies the separation process while improving the adsorption capacity and accelerating the adsorption rate. The adsorption capacity for BSA reached 390 ± 20 mg/g within 30 min. The introduction of CBMA segments on the surface after imprinting by amino-Michael addition makes its polymer chain length and position controllable. Under the strongest anti-nonspecific adsorption effect, MTCFs@SIP@CBMA exhibit excellent specific identification to BSA from mixed proteins. Additionally, MTCFs@SIP@CBMA show considerable reusability. Therefore, MTCFs@SIP@CBMA are expected to be applied in efficient separation of proteins in biological samples.     

Adsorption of bovine serum albumin protein onto amino‐containing thermosensitive core‐shell latexes

Adsorption of bovine serum albumin (BSA) onto positively charged core‐shell latex particles with a polystyrene core and a rich poly(N‐isopropylacrylamide) (NIPAM)) shell layer was investigated as a function of pH, ionic strength and temperature. Adsorption of BSA protein onto such cationic and thermosensitive particles was found negligible below the LCST of poly(NIPAM), whereas it was much higher above it. In addition, the pH and the salinity dependence of the adsorbed amount at the plateau reflected the role of electrostatic interactions. Protein adsorption behaviour was discussed by taking into account the changes in the interfacial properties of polymer particles (structure of the shell, hydrophilic–hydrophobic balance, charge density) versus temperature, suggesting that coulombic forces are mostly operating in this process. A desorption study showed that the BSA release efficiency was dependent upon the incubation time of the preliminary adsorbed step, and the effect of pH and ionic strength confirmed the contribution of electrostatic interactions. Copyright © 2004 Society of Chemical Industry     

Chitosan microspheres: modification of polymeric chem‐physical properties of spray‐dried microspheres to control the release of antibiotic drug

Antibiotic drug releasing from chitosan and acylchitosan microspheres was studied. The acylchitosan microspheres were prepared by modifying the microencapsulation process from spray‐drying to spray in‐liquid coagulating process for the improvement of chem‐physical properties of polymer in controlling the release of antibiotic drug. A higher yield of microspheres was recovered by this improved process. Crystallinity, swelling ability, and the morphology of various microspheres were investigated by X‐ray, water adsorption, and scanning electron microscopy studies. Results show that by modifying the microencapsulation process from spray‐drying to spray in‐liquid coagulating process, the chemical properties of the microsphere were varied from a hydrophilic chitosan microsphere to a hydrophobic acylchitosan microsphere, while the physical structure of the microsphere was varied from a porous chitosan microsphere to a dense acylchitosan microsphere. For the reasons, drug release rate of acylchitosan microspheres prepared by the novel spray microencapsulation method were apparently depressed, and the long‐acting release of antibiotic drug was possible to be achieved. © 1999 John Wiley & Sons, Inc. J Appl Polym Sci 71: 747–759, 1999     

A multiscale investigation on controlling bovine serum albumin adsorption onto polyurethane films

Our previous study on castor oil (CO) and poly(ethylene glycol) (PEG)‐based shape memory polyurethane (PU) films indicated that cell spreading on the polymer surface, cell morphology, and adhesion of fibroblast are closely related to the composition of the polymer that influences surface properties. This integrated experimental and computational study is designed to investigate the effect of important parameters such as surface roughness, crystallinity, hydrophilicity, distribution of hard/soft segments, and topology of the surface on protein adsorption for CO‐ and PEG‐based PUs. Analyses indicate that the crystallinity percentage highly promotes bovine serum albumin (BSA) adsorption. Roughness together with topological features determines BSA adsorption rate and concentration. Hydrophilicity and hard segment content seem to have less critical effect on adsorption. Distribution of hard segments into the soft segments emerges as another important factor for protein adsorption. © 2012 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2018 , 135, 45669.