Abstract：
: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 (5-10 min) formation of large (>2 μm) aggregates. sMyBP-C oligomers formed both at the initial 5-10 min and after 16 h of aggregation. Small angle X-ray scattering (SAXS) and DLS revealed sMyBP-C oligomers to consist of 7-10 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-β 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-S bonds providing for general stability.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Bobyleva LG,Shumeyko SA,Yakupova EI,Surin AK,Galzitskaya OV,Kihara H,Timchenko AA,Timchenko MA,Penkov NV,Nikulin AD,Suvorina MY,Molochkov NV,Lobanov MY,Fadeev RS,Vikhlyantsev IM,Bobylev AGdoi
10.3390/ijms22020731subject
Has Abstractpub_date
2021-01-13 00:00:00issue
2issn
1422-0067pii
ijms22020731journal_volume
22pub_type
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