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

ABSTRACT: 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. Graphical abstract Image 1 Highlights • These amino acid NPs displayed distinctly different affinity to human serum albumin, γ-globulin and fibrinogen respectively. •AArg@NPs, with great selectivity and specificity to fibrinogen, was potential to be a human fibrinogen-specific affinity reagent. •The negatively charged and hydrophobic D domain may be the predominant binding site of the positively charged and hydrophobic AArg@NPs to fibrinogen.

SUBMITTER: Zhu Y 

PROVIDER: S-EPMC8572708 | biostudies-literature |

REPOSITORIES: biostudies-literature