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Encapsulation of Protein-Polysaccharide HIP Complex in Polymeric Nanoparticles

机译:蛋白质-多糖HIP复合物在聚合物纳米粒子中的包封

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The objective of the present study is to formulate and characterize a nanoparticulate-based formulation of a macromolecule in a hydrophobic ion pairing (HIP) complex form. So far, HIP complexation approach has been studied only for proteins with molecular weight of 10–20 kDa. Hence, we have selected bovine serum albumin (BSA) having higher molecular weight (66.3 kDa) as a model protein and dextran sulphate (DS) as a complexing polymer to generate HIP complex. We have prepared and optimized the HIP complex formation process of BSA with DS. Ionic interactions between basic amino acids of BSA with sulphate groups of DS were confirmed by FTIR analysis. Further, nanoparticles were prepared and characterized with respect to size and surface morphology. We observed significant entrapment of BSA in nanoparticles prepared with minimal amounts of PLGA polymer. Finally, results of circular dichroism and intrinsic fluorescence assay have clearly indicated that HIP complexation and method of nanoparticle preparation did not alter the secondary and tertiary structures of BSA.
机译:本研究的目的是配制和表征疏水离子对(HIP)络合物形式的基于纳米粒子的大分子制剂。到目前为止,仅对分子量为10–20 kDa的蛋白质研究了HIP络合方法。因此,我们选择具有较高分子量(66.3 kDa)的牛血清白蛋白(BSA)作为模型蛋白,并选择硫酸葡聚糖(DS)作为络合聚合物以生成HIP络合物。我们已经准备并优化了BSA与DS的HIP配合物形成过程。通过FTIR分析证实了BSA的碱性氨基酸与DS的硫酸根之间的离子相互作用。此外,制备纳米颗粒并就尺寸和表面形态进行表征。我们观察到用最小量的PLGA聚合物制备的纳米颗粒中BSA的显着包埋。最后,圆二色性和固有荧光测定的结果清楚地表明,HIP络合和纳米颗粒的制备方法不会改变BSA的二级和三级结构。

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