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Дата последнего поиска статьи во внешних источниках: 9 апреля 2021 г.
Аннотация:A comparative study of amyloid properties of the aggregates of smooth muscle titin (SMT) from chicken gizzard wascarried out. These aggregates were formed in two solutions: 0.15 M glycine-KOH, pH 7.2–7.4 (SMT(Gly)) and 0.2 MKCl, 10 mM imidazole, pH 7.0 (SMT(KCl)). Electron microscopy data showed that SMT aggregates has an amorphousstructure in both cases. The results of atomic-force microscopy demonstrated slight differences in morphology in twotypes of aggregates. The SMT(Gly) aggregates were represented as branching chains, composed of spherical aggregatesapproximately 300–500 nm in diameter and up to 35 nm in height. The SMT(KCl) aggregates formed sponge-like structureswith strands of 8–10 nm in height. Structural analysis of SMT aggregates by X-ray diffraction revealed the presenceof cross-β-sheet structure in the samples under study. In the presence of SMT(Gly) aggregates, thioflavine Tfluorescence intensity was higher (~3-fold times) compared with that in the presence of SMT(KCl) aggregates. Congored-stained SMT(Gly) aggregates had yellow to apple-green birefringence under polarized light, which was not observedfor SMT(KCl) aggregates. Dynamic light scattering data showed the similar rate of aggregation for both types of aggregates,though SMT(KCl) aggregates were able to partially disaggregate under increased ionic strength of the solution.The ability of SMT to aggregation followed by disaggregation may be functionally significant in the cell.