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Updated: Jan 22, 2026

$Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies$

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Published on: April 11, 2021

Protein/Ice Interaction: High-Resolution Synchrotron X-ray Diffraction Differentiates Pharmaceutical Proteins from

Bakul Bhatnagar¹, Boris Zakharov^2,3, Alexander Fisyuk^4,5

¹BTx PharmSci Pharmaceutical R&D , Pfizer, Inc. , One Burtt Road , Andover 01810 , Massachusetts , United States.

The Journal of Physical Chemistry. B

|July 2, 2019

Summary

Pharmaceutical proteins significantly alter ice crystal properties, impacting protein stability. This study reveals distinct protein-ice interactions and potential mechanical stresses during freezing.

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Area of Science:

Biophysics
Materials Science
Crystallography

Background:

Understanding protein-ice interactions is crucial for cryopreservation and pharmaceutical formulation.
Previous studies have not fully elucidated the differential effects of various proteins on ice crystal formation.

Purpose of the Study:

To investigate protein-ice interactions using a novel X-ray diffraction (XRD) method.
To compare the impact of different proteins, including pharmaceutical proteins, on hexagonal ice (Ih) crystal properties.

Main Methods:

High-resolution synchrotron X-ray diffraction (XRD) was employed to analyze aqueous solutions of proteins and other solutes.
Characteristic features of XRD patterns of hexagonal ice (Ih) were measured to assess changes in crystalline domain size and microstrain.

Main Results:

Recombinant human albumin and monoclonal antibody (100 mg/mL) significantly reduced Ih crystalline domain size and increased microstrain.
Lysozyme (100 mg/mL) and an antifreeze protein (1 mg/mL) showed weaker effects on Ih.
Proteins did not exhibit preferential interaction with specific ice crystal faces, suggesting indirect interaction via the quasi-liquid layer.

Conclusions:

Pharmaceutical proteins indirectly interact with ice crystals, influencing their properties.
A minor population of ice crystals, possibly high-pressure forms (IceIII/IceIX), was detected, indicating mechanical stress involvement in protein destabilization during freezing.