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Updated: Mar 14, 2026

Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy

Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy

Published on: April 25, 2021

Amorphous protein aggregation monitored using fluorescence self-quenching.

Hiroki Jozawa¹, Md Golam Kabir¹, Tamotsu Zako²

¹Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, Koganei-shi, Japan.

|September 30, 2016

Summary

This study introduces a fluorescence method to monitor salt-induced amorphous protein aggregation, comparing it with light scattering techniques. Different peptide tags influence the aggregation kinetics and intermediate states of bovine pancreatic trypsin inhibitor variants.

Keywords:

SCP tag fluorescence self-quenching molecular condensation protein aggregation solubility

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Area of Science:

Biophysical chemistry
Protein aggregation
Biotechnology

Background:

Understanding amorphous protein aggregation is crucial for biotechnology.
Conventional methods like static light scattering (LS) and dynamic light scattering (DLS) are used to detect protein aggregation.
This study uses a bovine pancreatic trypsin inhibitor (BPTI) variant with different Solubility Controlling Peptide (SCP) tags to investigate aggregation.

Discussion:

Fluorescence self-quenching monitors time-dependent salt-induced amorphous aggregation.
LS and DLS signal changes vary based on SCP tag type (serine, alanine, aspartic acid).
Observations suggest an intermediate 'molecular condensation' phase preceding aggregation.

Key Insights:

Fluorescence monitoring provides a sensitive, real-time assessment of protein aggregation kinetics.
SCP tags modulate the transition from soluble states to amorphous aggregates.
The C5D tagged BPTI variant remains soluble, indicating effective solubility control.

Outlook:

This work advances the biophysical understanding of protein aggregation.
The developed fluorescence method can be applied to other protein systems.
Insights into aggregation intermediates can guide protein engineering for improved stability.