Decoupling Fluorous Protein Coatings Yield Heat-Stable and Intrinsically Sterile Bioformulations

ACS Appl Mater Interfaces. 2024 Jul 31;16(30):38893-38904. doi: 10.1021/acsami.4c03724. Epub 2024 Jul 16.

Abstract

Thermal inactivation is a major bottleneck to the scalable production, storage, and transportation of protein-based reagents and therapies. Failures in temperature control both compromise protein bioactivity and increase the risk of microorganismal contamination. Herein, we report the rational design of fluorochemical additives that promiscuously bind to and coat the surfaces of proteins to enable their stable dispersion within fluorous solvents. By replacing traditional aqueous liquids with fluorinated media, this strategy conformationally rigidifies proteins to preserve their structure and function at extreme temperatures (≥90 °C). We show that fluorous protein formulations resist contamination by bacterial, fungal, and viral pathogens, which require aqueous environments for survival, and display equivalent serum bioavailability to standard saline samples in animal models. Importantly, by designing dispersants that decouple from the protein surface in physiologic solutions, we deliver a fluorochemical formulation that does not alter the pharmacologic function or safety profile of the functionalized protein in vivo. As a result, this nonaqueous protein storage paradigm is poised to open technological opportunities in the design of shelf-stable protein reagents and biopharmaceuticals.

Keywords: biotherapeutics; fluorine chemistry; perfluorocarbon; protein formulation; protein stability; protein structure.

MeSH terms

  • Animals
  • Coated Materials, Biocompatible / chemistry
  • Coated Materials, Biocompatible / pharmacology
  • Hot Temperature*
  • Mice
  • Proteins / chemistry
  • Proteins / metabolism

Substances

  • Proteins
  • Coated Materials, Biocompatible