Fc Domain-Imprinted Stealth Nanogels Capable of Orientational Control of Immunoglobulin G Adsorbed In Vivo

ACS Appl Mater Interfaces. 2022 Apr 13;14(14):16074-16081. doi: 10.1021/acsami.2c01953. Epub 2022 Mar 30.

Abstract

Regulation of nanomaterial-cell interaction is an important requisite for a variety of biomedical applications such as drug delivery systems and theranostics. Here, we demonstrate the regulation of nanomaterial-cell interaction using the oriented adsorption of intrinsic immunoglobulin G (IgG) on molecularly imprinted polymer nanogels (MIP-NGs) capable of recognizing the fragment crystallizable (Fc) domain of IgG. The unique domain recognition property resulted in the suppression of the immune response in Fc domain receptor-possessing macrophages and natural killer cells due to the regulation of protein corona based on the oriented adsorption of IgG. This resulted in the hindrance of the Fc domain, which is the trigger of an immune response. Furthermore, the acquisition of stealth capability was successfully demonstrated in vivo using intravital confocal laser scanning microscopy. The domain imprinting proposed in this study will provide a new strategy for creating nanomaterials capable of domain recognition-based oriented adsorption of intrinsic proteins in situ, thus regulating the protein corona formed on the nanomaterials. Thus, the unique Fc domain-recognition nanomaterial developed in our study can be used for various biomedical applications to target specific cells without triggering an immune response.

Keywords: Fc domain; immunoglobulin G; molecularly imprinted polymer nanogels; protein corona.

MeSH terms

  • Adsorption
  • Immunoglobulin G
  • Molecular Imprinting* / methods
  • Nanogels
  • Protein Corona*

Substances

  • Immunoglobulin G
  • Nanogels
  • Protein Corona