Abstract
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.
Highlights
Antibodies represent highly specific and high binding affinity biomolecular recognition elements for diagnostic assays, biosensors, and therapeutics, but are sensitive to denaturation and degradation
Water is essential for stabilizing biomolecular structures through hydrogen bonding, providing proton donors/acceptors, regulating binding interactions, and controlling molecular dynamics; but, at the same time, water is very detrimental to biomolecular structure and function by increasing the rate of hydrolysis and oxidation, destabilizing and disrupting protein structure, and increasing the susceptibility/sensitivity to elevated temperatures
Polyclonal rabbit anti-ferritin immunoglobulin G antibodies or IgG antibodies obtained from rabbit serum (IgG) were cationized by the addition of N,N-dimethyl-1,3-propanediamine (DMPDA) in the presence of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) coupling reagent in order to modify carboxyl containing amino acids with positive charges
Summary
Antibodies represent highly specific and high binding affinity biomolecular recognition elements for diagnostic assays, biosensors, and therapeutics, but are sensitive to denaturation and degradation. 1234567890():,; The successful integration of biological materials in biosensors, diagnostics, biomedical devices, and other abiotic materials (e.g., plastics) is severely limited by the poor stability of biomolecules, low tolerance to elevated temperatures, and increased sensitivity and incompatibility issues due to different processing conditions (i.e., pH, salts, solvents) resulting in loss of biofunctionality. In all, these issues restrict the utilization of biological materials in operational and real-world settings without the use of strictly controlled environmental conditions (e.g., refrigeration) and/or the need for multiple processing steps. Water-free antibody liquids exhibited >60% binding activity after repeated heating to 125 °C and facilitated the creation of antibody-based hot glue materials
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