Effect of Complex Coacervation with Hyaluronic Acid on Protein Transition in a Subcutaneous Injection Site Model System

Chem Pharm Bull (Tokyo). 2020;68(11):1109-1112. doi: 10.1248/cpb.c20-00585.

Abstract

The occurrence of complex coacervation in an aqueous mixture of proteins (lysozyme, albumin, immunoglobulin G) and hyaluronic acid and its effect on protein transition in a model system was studied to elucidate factors determining the bioavailability of subcutaneously injected therapeutic proteins. Mixing of hyaluronic acid and the model proteins induced complex coacervation at solution pH close to or below the isoelectric point of the proteins. In vitro dialysis using membranes with large pore size tube represented a limitation in the protein transition of the coacervation mixture. Thermal analysis suggested there was retention of the protein conformation in the polymer complex.

Keywords: bioavailability; coacervation; subcutaneous injection.

MeSH terms

  • Animals
  • Calorimetry, Differential Scanning
  • Cattle
  • Humans
  • Hyaluronic Acid / chemistry*
  • Hyaluronic Acid / metabolism
  • Hydrogen-Ion Concentration
  • Immunoglobulin G / chemistry*
  • Immunoglobulin G / metabolism
  • Models, Molecular*
  • Muramidase / chemistry*
  • Muramidase / metabolism
  • Protein Conformation
  • Serum Albumin / chemistry*
  • Serum Albumin / metabolism
  • Temperature

Substances

  • Immunoglobulin G
  • Serum Albumin
  • Hyaluronic Acid
  • Muramidase