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Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

Updated: Jun 27, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Profiling Protein Aggregate Size Using Single-Molecule Array Technology.

Dorothea Böken^1,2, Yunzhao Wu^1,2, Jianli Zhang³

¹Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Analytical Chemistry

|June 25, 2026

Summary

This summary is machine-generated.

New methods using single-molecule array (Simoa) brightness reveal protein aggregate size differences in Alzheimer's disease. This technique offers insights into neurodegenerative disease mechanisms and protein aggregation dynamics.

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Area of Science:

Biochemistry
Neuroscience
Biotechnology

Background:

Protein aggregation is a hallmark of neurodegenerative diseases.
Current methods for characterizing aggregate size in biological samples are limited.

Purpose of the Study:

To demonstrate that fluorescence intensity in single-molecule array (Simoa) microwells provides size-dependent information about protein aggregates.
To apply this novel method to analyze tau aggregate size in Alzheimer's disease.

Main Methods:

Utilized defined synthetic tau assemblies to correlate aggregate size with Simoa microwell fluorescence intensity (brightness).
Applied Simoa brightness profiling to human brain homogenates from Alzheimer's disease patients and controls.
Validated findings using single-molecule super-resolution microscopy.
Assessed dynamic changes in protein aggregation in a neuronal cell model.

Main Results:

Increasing aggregate size correlated with higher Simoa microwell brightness.
Alzheimer's disease brain homogenates showed a shift towards larger tau aggregates compared to controls.
Simoa brightness profiling detected time-dependent increases in aggregate size in a cell model.
The method robustly reported population-level shifts in aggregate size distributions.

Conclusions:

Simoa microwell brightness serves as a valuable proxy for protein aggregate size.
This repurposed technology offers high-throughput structural insights into protein aggregation in neurodegenerative diseases.
Simoa brightness profiling enhances the understanding of aggregation dynamics and disease mechanisms.