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

• Main Authors: Liu, R. (Author), Shea, K.J (Author), Wu, D. (Author), Yu, Q. (Author), Zhu, Q. (Author), Zhu, Y. (Author)
• Format: Article
• Language: English
• Published: Xi'an Jiaotong University 2021
• Subjects: Affinity reagent; amino acid; Amino-acid monomers; aqueous solution; arginine; Arginine; Article; binding affinity; fibrinogen; Fibrinogen; glutamic acid; human serum albumin; hydrophobicity; immunoglobulin; immunoprecipitation; incubation time; leucine; lysine; molecular docking; phenylalanine; poly(n isopropylacrylamide); polymer nanoparticle; protein domain; Protein interaction; Synthetic polymer nanoparticles
• Online Access: View Fulltext in Publisher

 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. © 2020 Xi'an Jiaotong University