Creation of stable water-free antibody based protein liquids

• Published in: Communications materials 2021-12, Vol.2 (1), p.1-11, Article 118
• Main Authors: Slocik, Joseph M., Dennis, Patrick B., Kuang, Zhifeng, Pelton, Anthony, Naik, Rajesh R.
• Format: Article
• Language: English
• Subjects: 13/1; 631/61/51; 639/301/54; 82/103; 96/63; Antibodies; Antigens; Binding; Bioengineering; Biomolecules; Biosensors; Biotransformation; Chemistry and Materials Science; Denaturation; Heating; IgG antibody; Ion pairs; Liquids; Materials Science; Proteins; Thermal cycling; Thermoplastic resins
• ISSN: 2662-4443; 2662-4443
• DOI: 10.1038/s43246-021-00222-2

Antibodies represent highly specific and high binding affinity biomolecular recognition elements for diagnostic assays, biosensors, and therapeutics, but are sensitive to denaturation and degradation. Consequently, the combination of existing in a hydrated state with a large and complex biomolecular structure results in loss of antibody-antigen binding, limited shelf-life, and decreased sensor response over time and under non-optimal conditions. The development and use of water-free protein liquids has led to stabilization of labile biomolecules, solvents for biotransformation reactions, and formation of new bio-composites with incompatible materials. Here, we exploit the polycationic nature of modified antibodies and their ability to form ion pairs for the conversion of primary Immunoglobulin G antibodies into stable protein liquids that retained more than 60% binding activity after repeated heating up to 125 °C, and demonstrate compatibility with thermoplastics. Antibodies are widely used in biotechnology and bioengineering, but are sensitive to their environment. Here, primary antibodies are converted into thermally-stable protein liquids, achieving >60% antigen binding after cyclic heating at 125 °C and remain active when incorporated into plastics.