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Related Concept Videos

Transcytosis of IgG01:15

Transcytosis of IgG

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Related Experiment Video

Updated: May 7, 2026

Phase Behavior of Charged Vesicles Under Symmetric and Asymmetric Solution Conditions Monitored with Fluorescence Microscopy
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Published on: October 24, 2017

Phase transitions in human IgG solutions.

Ying Wang1, Aleksey Lomakin, Ramil F Latypov

  • 1Materials Processing Center, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.

The Journal of Chemical Physics
|October 5, 2013
PubMed
Summary
This summary is machine-generated.

Researchers studied the phase behavior of immunoglobulin G (IgG) solutions, revealing unique liquid-liquid phase separation properties. These findings are crucial for understanding IgG-related diseases and improving antibody drug formulations.

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Materials Science

Background:

  • Protein condensations like crystallization and phase separation occur in concentrated antibody solutions.
  • While most Immunoglobulin G (IgG) antibodies are soluble, some can condense under physiological conditions, impacting diseases and biopharmaceuticals.
  • The phase behavior of IgG solutions is poorly understood due to high solubility, yet is key for non-spherical protein studies.

Purpose of the Study:

  • To investigate the hidden phase transitions in concentrated IgG solutions below their freezing point.
  • To explore the liquid-liquid phase separation (LLPS) of various human myeloma and recombinant pharmaceutical IgGs.
  • To examine the relationship between crystallization and LLPS in human cryoglobulin IgGs.

Main Methods:

  • Developed an experimental approach to study IgG solutions with phase transitions below the freezing point.
  • Investigated LLPS in six human myeloma IgGs and two recombinant pharmaceutical human IgGs.
  • Studied the crystallization and LLPS relationship in two human cryoglobulin IgGs.

Main Results:

  • The coexistence curve shape for IgGs differs from quasi-spherical proteins, but is similar across all tested IgGs.
  • All IgGs exhibited critical points around ~100 mg/ml, with significant variations in critical temperatures.
  • LLPS in IgG solutions was found to be metastable relative to crystallization.

Conclusions:

  • IgG phase behavior is governed by near-identical molecular geometry and diverse inter-protein interaction energies.
  • Findings provide a basis for further research into generic IgG phase behavior and outlier condensations.
  • Understanding IgG phase diagrams is vital for immunoglobulin deposition diseases and colloidal stability of IgG pharmaceuticals.