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• W4313509478 endingPage "1056" @default.
• W4313509478 startingPage "1056" @default.
• W4313509478 abstract "A giant multidomain protein of striated and smooth vertebrate muscles, titin, consists of tandems of immunoglobulin (Ig)- and fibronectin type III (FnIII)-like domains representing β-sandwiches, as well as of disordered segments. Chicken smooth muscles express several titin isoforms of ~500–1500 kDa. Using various structural-analysis methods, we investigated in vitro nonspecific amyloid aggregation of the high-molecular-weight isoform of chicken smooth-muscle titin (SMTHMW, ~1500 kDa). As confirmed by X-ray diffraction analysis, under near-physiological conditions, the protein formed amorphous amyloid aggregates with a quaternary cross-β structure within a relatively short time (~60 min). As shown by circular dichroism and Fourier-transform infrared spectroscopy, the quaternary cross-β structure—unlike other amyloidogenic proteins—formed without changes in the SMTHMW secondary structure. SMTHMW aggregates partially disaggregated upon increasing the ionic strength above the physiological level. Based on the data obtained, it is not the complete protein but its particular domains/segments that are likely involved in the formation of intermolecular interactions during SMTHMW amyloid aggregation. The discovered properties of titin position this protein as an object of interest for studying amyloid aggregation in vitro and expanding our views of the fundamentals of amyloidogenesis." @default.
• W4313509478 created "2023-01-06" @default.
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• W4313509478 date "2023-01-05" @default.
• W4313509478 modified "2023-10-17" @default.
• W4313509478 title "Nonspecific Amyloid Aggregation of Chicken Smooth-Muscle Titin: In Vitro Investigations" @default.
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• W4313509478 doi "https://doi.org/10.3390/ijms24021056" @default.
• W4313509478 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36674570" @default.
• W4313509478 hasPublicationYear "2023" @default.
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