Engineered polymer nanoparticles incorporating L-amino acid groups as affinity reagents for fibrinogen

作者：Zhu, Yongyan; Liu, Ruixuan; Wu, Dengyu; Yu, Qianqian; Shea, Kenneth J.^*; Zhu, Quanhong^*

来源：Journal of Pharmaceutical Analysis, 2021, 11(5): 596-602.

DOI：10.1016/j.jpha.2020.10.004

• Synthetic polymer nanoparticles
• Amino-acid monomers
• Arginine
• Fibrinogen
• Affinity reagent
• Protein interaction

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, g-globulin, and human serum albumin (HSA) respectively, the NPs that incorporated Nacryloyl-Arg monomers (AArg@NPs) showed the strongest and most specific binding affinity to fibrinogen, when compared with g-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.

• 单位
  南方医科大学