Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro

Autor: Mariya Yu. Suvorina, A. G. Bobylev, A. A. Timchenko, Sergey A Shumeyko, Ivan M. Vikhlyantsev, R. S. Fadeev, Alexey K. Surin, Maria Timchenko, Oxana V. Galzitskaya, Mikhail Yu. Lobanov, Alexey D. Nikulin, Elmira I Yakupova, Nikolay V Molochkov, L. G. Bobyleva, Hiroshi Kihara, Nikita V. Penkov
Jazyk: angličtina
Rok vydání: 2021
Předmět:
0301 basic medicine
Models
Molecular
Circular dichroism
Protein Conformation
Protein aggregation
Mass Spectrometry
lcsh:Chemistry
chemistry.chemical_compound
0302 clinical medicine
X-Ray Diffraction
Protein secondary structure
lcsh:QH301-705.5
Spectroscopy
Chromatography
High Pressure Liquid
Small-angle X-ray scattering
Chemistry
Circular Dichroism
muscle proteins
amyloid
General Medicine
SAXS
Computer Science Applications
CD
Monomer
Myosin binding
Amyloid
DLS
In Vitro Techniques
Protein Aggregation
Pathological
Catalysis
Article
protein aggregation
Inorganic Chemistry
03 medical and health sciences
Protein Aggregates
Structure-Activity Relationship
Dynamic light scattering
Amino Acid Sequence
structural analysis
Physical and Theoretical Chemistry
Molecular Biology
MyBP-C
amyloid-like aggregation
Organic Chemistry
Dynamic Light Scattering
Kinetics
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
Biophysics
Carrier Proteins
030217 neurology & neurosurgery
Zdroj: International Journal of Molecular Sciences, Vol 22, Iss 731, p 731 (2021)
International Journal of Molecular Sciences
Volume 22
Issue 2
ISSN: 1661-6596
1422-0067
Popis: This work investigated in vitro aggregation and amyloid properties of skeletal myosin binding protein-C (sMyBP-C) interacting in vivo with proteins of thick and thin filaments in the sarcomeric A-disc. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) found a rapid (5&ndash
10 min) formation of large (>
2 &mu
m) aggregates. sMyBP-C oligomers formed both at the initial 5&ndash
10 min and after 16 h of aggregation. Small angle X-ray scattering (SAXS) and DLS revealed sMyBP-C oligomers to consist of 7&ndash
10 monomers. TEM and atomic force microscopy (AFM) showed sMyBP-C to form amorphous aggregates (and, to a lesser degree, fibrillar structures) exhibiting no toxicity on cell culture. X-ray diffraction of sMyBP-C aggregates registered reflections attributed to a cross-&beta
quaternary structure. Circular dichroism (CD) showed the formation of the amyloid-like structure to occur without changes in the sMyBP-C secondary structure. The obtained results indicating a high in vitro aggregability of sMyBP-C are, apparently, a consequence of structural features of the domain organization of proteins of this family. Formation of pathological amyloid or amyloid-like sMyBP-C aggregates in vivo is little probable due to amino-acid sequence low identity (<
26%), alternating ordered/disordered regions in the protein molecule, and S&ndash
S bonds providing for general stability.
Databáze: OpenAIRE
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