Related Experiment Video
Updated: Jun 10, 2026

12:58
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
Published on: September 12, 2019
Nanoimaging for protein misfolding diseases
Yuri L Lyubchenko1, Bo-Hyun Kim, Alexey V Krasnoslobodtsev
1Department of Pharmaceutical Sciences, University of Nebraska Medical Center, Omaha, NE 68198-6025, USA. ylyubchenko@unmc.edu
Summary
Protein misfolding and aggregation cause neurodegenerative diseases like Alzheimer's. Novel biophysical techniques are advancing our understanding of these processes and potential treatments.
Area of Science:
- Biophysics
- Neuroscience
- Molecular Biology
Background:
- Protein misfolding and aggregation are implicated in neurodegenerative diseases such as Parkinson's, Alzheimer's, and Huntington's.
- Specific protein aggregates are linked to distinct diseases, causing neuronal dysfunction and loss.
- The propensity for protein aggregation is a general characteristic, often involving transiently misfolded intermediates.
Purpose of the Study:
- To review the impact of recent studies on understanding protein self-assembly mechanisms.
- To discuss the development of treatments for protein misfolding-related diseases.
- To address fundamental unanswered questions regarding the formation and importance of misfolded protein conformations.
Main Methods:
- Review of existing literature utilizing X-ray crystallography, nuclear magnetic resonance, electron microscopy, and atomic force microscopy.
- Application of novel ensemble methods and single-molecule biophysics techniques to study protein misfolding.
- Analysis of studies investigating the conditions leading to protein misfolding and disease-prone complex formation.
Main Results:
- Traditional methods provided structural insights into protein aggregates.
- Emerging ensemble and single-molecule techniques offer new perspectives on transient misfolded states.
- Understanding the precise conditions for misfolding remains a challenge, complicating disease prevention.
Conclusions:
- Recent advances in biophysics are crucial for deciphering protein self-assembly mechanisms.
- Further research is needed to clarify the causes of protein misfolding and develop effective disease preventions.
- These insights are vital for the development of novel therapeutic strategies against neurodegenerative disorders.
Related Concept Videos
Protein Folding
Overview
Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Dynamics in Living Cells
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

