Protein aggregation is a critical quality attribute that may increase the risk of immune response. Protein aggregates can form during production, storage or shipment. Many environmental conditions (e.g., mechanical stress, pH, ionic strength, temperature, light or oxidation) lead to protein unfolding, misfolding and aggregation by physical interaction or covalent bonding.

Our scientists have extensive experience in characterization of aggregates in solution, including proteins/peptides, oligonucleotides and other polymers. We employ a complete suite of 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