Protein aggregation has been a critical quality attribute and is considered an important factor that may increase the risk of immune response.  Protein aggregates can form during production, storage, or shipment.  Many environmental conditions (i.e., mechanical stress, pH, ionic strength, temperature, light, and oxidation) lead to protein unfolding, misfolding, and subsequently to aggregation either by physical interaction or by covalent bonding.  SSCI has extensive experience in characterization of aggregates in solution including proteins/peptides, oligonucleotides, and other polymers using the advanced analytical techniques:

  • SEC-MALS and GPC (gel permeation chromatography) for molecular weight estimation
  • DLS for particle size (hydrodynamic radius)
  • SEM for particle morphology
  • Native/SDS-PAGE and IEF for molecular weight and isoelectric point
  • IR microscopy and NMR spectroscopy for probing conformational changes
  • Near- and far-UV circular dichroism spectrophotometry for high order structural analyses
  • Free sulfhydryl group determination