Low-Ionic Antibody Composition for Fc Protein Stability

The patent applies parameter changes by reducing buffer concentration from conventional levels (typically 10-50 mM) to low levels (0-5 mM), and by adjusting ionic strength to low levels (<20 mM). This parameter optimization resolves the contradiction by finding a buffer concentration range that provides sufficient pH stability while minimizing protein degradation, specifically showing that 0-5 mM buffer concentration with low ionic strength maintains both pH control and protein stability for Fc domain-containing constructs

The patent employs self-buffering capacity of the protein construct itself as a copy of the buffering function. The Fc domain-containing protein constructs possess intrinsic buffering能力 through their amino acid side chains, which can maintain pH stability without requiring high concentrations of external buffers. This copying approach eliminates the need for large amounts of conventional buffers while still achieving pH control, thereby resolving the contradiction between pH stability and protein degradation

The patent applies parameter changes by optimizing pH and ionic strength parameters to achieve enhanced protein stability at elevated temperatures. By formulating with low buffer concentration (0-5 mM) and low ionic strength (<20 mM), the patent enables Fc domain-containing constructs to maintain stability at 25°C or 30°C for extended periods, thereby eliminating the need for refrigeration and improving storage convenience while preserving protein stability

The patent enables the protein formulation to function as a stable, disposable product that does not require expensive refrigeration infrastructure. By achieving stability at room temperature through optimized formulation parameters, the product can be stored and transported under simpler, more convenient conditions, effectively replacing the need for continuous cold chain maintenance