Mass Photometry

Label-free protein oligomer detection

Principle of Operation

Mass photometry quantifies the interference between light reflected from a glass surface and light scattered by individual biomolecules transiently interacting with that surface.
The resulting contrast signal scales directly with molecular mass (Young et al., 2018), enabling accurate mass determination without labels or immobilization.

Applications

Protein State & Stability

  • Oligomeric state determination (monomer → higher-order assemblies)
  • Buffer and pH dependent stability profiling
  • Assessment of stabilizing/destabilizing compound effects

Complex Formation

  • Label-free detection of binary and ternary complexes, including those induced by bivalent compounds and molecular glues
  • Quantification of compound-driven complex formation
  • pH dependent complex formation analysis

  • Stability-monitoring of biomolecular complexes

     

Antibody & Nucleic Acid Systems

  • Fragmentation and aggregation analysis
  • Antibody–antigen binding assessment
  • Protein–nucleic acid complex characterization

 

Key Advantages

  • Native, in solution measurements
  • Label-free detection
  • Sensitive to sample heterogeneity and purity
  • Minimal sample consumption (100 pM–100 nM)
  • Broad mass range: 30 kDa–5 MDa
  • Time-resolved measurements for dynamic processes
  • Suitable for oligomerization and complex formation studies
  • Compatible with membrane proteins
  • Rapid data acquisition and turnaround

Mass photometry output showing formation of dimers as the protein concentration increases

Example output showing protein dimer formation as concentration increases