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Published on: December 5, 2013
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Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.
Liya G Bobyleva1, Sergey A Shumeyko1, Elmira I Yakupova1
1Laboratory of the Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.
International Journal of Molecular Sciences
|January 16, 2021
Summary
Skeletal myosin binding protein-C (sMyBP-C) rapidly forms large aggregates in vitro. These amyloid-like structures show no cell toxicity, and in vivo aggregation is unlikely due to protein stability factors.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Skeletal myosin binding protein-C (sMyBP-C) is crucial for sarcomere structure and function.
- Understanding sMyBP-C's aggregation properties is important for muscle physiology and disease research.
Purpose of the Study:
- To investigate the in vitro aggregation properties and amyloid characteristics of skeletal myosin binding protein-C (sMyBP-C).
- To assess the potential for sMyBP-C to form pathological amyloid aggregates in vivo.
Main Methods:
- Dynamic light scattering (DLS) and transmission electron microscopy (TEM) for aggregate size and morphology.
- Small angle X-ray scattering (SAXS) for oligomer composition.
- Atomic force microscopy (AFM) and X-ray diffraction for structural analysis.
- Circular dichroism (CD) for secondary structure changes.
Main Results:
- Rapid formation of large (>2 μm) sMyBP-C aggregates within 5-10 minutes in vitro.
- Oligomers composed of 7-10 monomers were identified.
- Amorphous and fibrillar aggregates were observed, with no detected cell toxicity.
- X-ray diffraction confirmed a cross-β quaternary structure, indicative of amyloid-like properties.
- Amyloid-like structure formation occurred without altering sMyBP-C's secondary structure.
Conclusions:
- sMyBP-C exhibits high in vitro aggregability, likely due to its domain organization.
- In vivo formation of pathological amyloid or amyloid-like sMyBP-C aggregates is improbable.
- Protein stability is maintained by factors including low sequence identity with known amyloidogenic proteins, alternating ordered/disordered regions, and disulfide bonds.
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