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Updated: Jul 7, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
Published on: September 12, 2019
Physical and chemical perturbations induce the formation of protein aggregates with different structural features
Antonino Natalello1, Rachel Santarella, Silvia Maria Doglia
1Dipartimento di Biotecnologie e Bioscienze, Universita' degli Studi Milano-Bicocca, Piazza della Scienza 2, 20126 Milano, Italy.
Abstract:
The in vitro aggregation of the model GST-GFP fusion protein was induced by several effectors, including those mimicking variations occurring under cell stress conditions. In particular, we examined the effects of thermal treatments, redox state and pH variations, salt addition, and freezing and thawing cycles. The resulting aggregates displayed different morphologies as seen by electron microscopy, and different secondary and tertiary structures, as indicated by Fourier transform infrared spectroscopy and fluorescence. Therefore, proteins can be forced to undergo multiple aggregation pathways that lead to assemblies with different molecular structures and, possibly, specific physiological and pathological roles. In conclusion, great caution should be taken in inferring conclusions on protein aggregation and disaggregation in vivo from results obtained using aggregates produced under non-physiological perturbations.
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