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Engineered polymer nanoparticles incorporating l-amino acid groups as affinity reagents for fibrinogen
Journal of Pharmaceutical Analysis ( IF 6.1 ) Pub Date : 2020-10-22 , DOI: 10.1016/j.jpha.2020.10.004
Yongyan Zhu 1, 2, 3 , Ruixuan Liu 1 , Dengyu Wu 1 , Qianqian Yu 1 , Kenneth J Shea 4 , Quanhong Zhu 1, 2, 3
Affiliation  

Synthetic polymer hydrogel nanoparticles (NPs) were developed to function as abiotic affinity reagents for fibrinogen. These NPs were made using both temperature-sensitive N-isopropyl acrylamide (NIPAm) and l-amino acid monomers. Five kinds of l-amino acids were acryloylated to obtain functional monomers: l-phenylalanine (Phe) and l-leucine (Leu) with hydrophobic side chains, l-glutamic acid (Glu) with negative charges, and l-lysine (Lys) and l-arginine (Arg) with positive charges. After incubating the NPs with fibrinogen, γ-globulin, and human serum albumin (HSA) respectively, the NPs that incorporated N-acryloyl-Arg monomers (AArg@NPs) showed the strongest and most specific binding affinity to fibrinogen, when compared with γ-globulin and HSA. Additionally, the fibrinogen-AArg binding model had the best docking scores, and this may be due to the interaction of positively charged AArg@NPs and the negatively charged fibrinogen D domain and the hydrophobic interaction between them. The specific adsorption of AArg@NPs to fibrinogen was also confirmed by the immunoprecipitation assay, as the AArg@NPs selectively trapped the fibrinogen from a human plasma protein mixture. AArg@NPs had a strong selectivity for, and specificity to, fibrinogen and may be developed as a potential human fibrinogen-specific affinity reagent.



中文翻译:

工程化的聚合物纳米粒子包含 l-氨基酸基团作为纤维蛋白原的亲和试剂

合成聚合物水凝胶纳米粒子 (NPs) 被开发用作纤维蛋白原的非生物亲和试剂。这些纳米颗粒是使用温度敏感的 N-异丙基丙烯酰胺 (NIPAm) 和l-氨基酸单体制成的。五种l-氨基酸被丙烯酰化得到功能单体:l-苯丙氨酸(Phe)和l-亮氨酸(Leu)具有疏水侧链,l-谷氨酸(Glu)带负电荷,l-赖氨酸(Lys)和l-精氨酸 (Arg) 带正电荷。将 NPs 分别与纤维蛋白原、γ-球蛋白和人血清白蛋白 (HSA) 孵育后,与 γ 相比,掺入 N-丙烯酰-精氨酸单体 (AArg@NPs) 的 NPs 对纤维蛋白原表现出最强和最特异性的结合亲和力-球蛋白和 HSA。此外,纤维蛋白原-AArg 结合模型的对接得分最高,这可能是由于带正电的 AArg@NPs 与带负电的纤维蛋白原 D 结构域的相互作用以及它们之间的疏水相互作用。AArg@NPs 对纤维蛋白原的特异性吸附也通过免疫沉淀试验得到证实,因为 AArg@NPs 选择性地从人血浆蛋白混合物中捕获纤维蛋白原。AArg@NPs 具有很强的选择性和特异性,

更新日期:2020-10-22
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