Related Experiment Video

Updated: Nov 21, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.4K

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
PubMed

Insights

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.
Keywords:
CDDLSMyBP-CSAXSX-ray diffractionamyloidamyloid-like aggregationmuscle proteinsprotein aggregationstructural analysis

More Related Videos

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

3.5K
Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells11:12

Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells

Published on: October 4, 2017

7.5K

Related Concept Videos

Amyloid Fibrils03:03

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,...
11.2K
Amyloid Fibrils03:03

Amyloid Fibrils

6.1K
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
84.7K
Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well...
5.5K