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Related Experiment Video

Updated: Nov 21, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

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.

Keywords:

CD DLS MyBP-C SAXS X-ray diffraction amyloid amyloid-like aggregation muscle proteins protein aggregation structural analysis

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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.