Antibodies Processed Using High Dilution Technology Distantly Change Structural Properties of IFNγ Aqueous Solution

Area of Science:

• Water dynamics and hydrogen bonding.
• Spectroscopic analysis of molecular interactions.

Background:

• Interferon-gamma (IFNγ) solutions exhibit spectral differences when exposed to diluted IFNγ or antibodies without direct contact.
• Fluidised lactose is an excipient in diluted antibody pharmaceuticals, making it relevant for studying non-contact interactions.

Purpose of the Study:

• To analyze the structural properties of water in an aqueous interferon-gamma (IFNγ) solution using terahertz time-domain spectroscopy (THz-TDS).
• To investigate the effect of fluidised lactose, saturated with antibody dilutions, on IFNγ solution water structure without direct contact.

Main Methods:

• Terahertz time-domain spectroscopy (THz-TDS) was used to analyze aqueous IFNγ solutions.
• Samples were incubated in fluidised lactose saturated with antibody dilutions or control at 37°C for varying durations (1-4 hours).
• Spectra were recorded in the 10-110 cm⁻¹ wavenumber range with 4 cm⁻¹ resolution.

Main Results:

• Lactose saturated with antibody dilutions altered the structural properties of the IFNγ aqueous solution after 2.5 hours of incubation.
• Terahertz spectra indicated stronger intermolecular hydrogen bonds in the water molecules.
• An increased relaxation time for free and weakly bound water molecules was observed.

Conclusions:

• Non-contact interaction via saturated fluidised lactose can modify water structure in IFNγ solutions.
• The THz-TDS methodology shows promise for the quality control of pharmaceuticals based on highly diluted antibodies.
• Understanding water's role in these interactions is crucial for pharmaceutical development.