Apomyoglobin mutants with single point mutations at Val10 can form amyloid structures at permissive temperature

Katina, N. S.; Ilyina, Nelly B.; Kashparov, I. A.; Balobanov, Vitaly A.; Vasiliev, V.D.; Bychkova, Valentina E.

doi:10.1134/s0006297911050051

Cited by 11 publications

(11 citation statements)

References 37 publications

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“…Stability of the studied proteins was taken as a pH value which corresponds to the middle of pH‐induced transition from the native to intermediate state monitored by changes in intensity at 222 nm in far UV CD spectra presented in Figure 5 (see also9).…”

Section: Results and Disscussionmentioning

confidence: 99%

“…Substantial progress in understanding of amyloid formation was achieved during the last decade 3–5. However, there are few reports on time‐dependent structural changes occurring in protein aggregates during their formation 6–9. It should be emphasized that many studies were performed under denaturing conditions, and only some of them used native‐like conditions similar to those existing in the cell 9–11.…”

Section: Introductionmentioning

confidence: 99%

“…However, there are few reports on time‐dependent structural changes occurring in protein aggregates during their formation 6–9. It should be emphasized that many studies were performed under denaturing conditions, and only some of them used native‐like conditions similar to those existing in the cell 9–11. This work was aimed to study kinetics of protein aggregation by a variety of techniques and the relationship between structural protein stability and the ability to form amyloids.…”

Section: Introductionmentioning

confidence: 99%

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Kinetics of Mutant Apomyoglobin Association

Katina

Timchenko

Kihara

et al. 2012

Macromolecular Symposia

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Association of protein molecules in human tissues underlies many diseases, which brings it in the focus of numerous studies. Previous reports described amyloid formation with the unfolded protein state taken as the starting point. Here, we present kinetics of protein aggregation starting from the protein native state and with consideration of its structural stability. We constructed mutant forms of apomyoglobin (apoMb) and investigated them by light scattering, small-angle Xray scattering (SAXS), transmission electron microscopy (TEM), atomic force microscopy (AFM), fluorescence, far UV CD and FTIR spectroscopy. We found that apoMb mutants formed aggregates that changed their shape after 24 h incubation at a physiologically relevant temperature of 40 8C, pH 5.5, from almost globular (micellar) to elongated and curly. The elongated particles exhibited properties of the cross-beta structure characteristic of amyloids. According to SAXS, the elongated aggregates were not less than 300 Å in length, the gyration radius of their cross-section (R c ) was about 35 Å, and their molecular mass was over 400 kDa. An elongated shape of the aggregates was also demonstrated by TEM-and AFM imaging. The ability of apoMb mutants to form elongated amyloid-like aggregates, as well as their compactness, negatively correlated with stability of their native structure.

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Section: Results and Disscussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Kinetics of Mutant Apomyoglobin Association

Katina

Timchenko

Kihara

et al. 2012

Macromolecular Symposia

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“…Известно, что многие пептиды и белки способны образовывать агрегаты амилоидного типа при нейтральных значениях pH буферного раствора [13][14][15]. В то же время изменение pH раствора может активировать разворачивание и фибриллогенез белков, а также влиять на морфологию фибрилл [16][17][18]. Изменение pH с 7.5 до 2.0 не приводило к образованию фибрилл для целого белка S1 (неопубликованные данные).…”

Section: Introductionunclassified

Investigation of Fibrillation by Amyloidogenic Regions of the Ribosomal S1 Proteins

Deryusheva¹,

Мачулин²,

Selivanova³

et al. 2020

Proceedings of the International Conference "Mathematical Biology and Bioinformatics"

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RNA-binding structural S1 domain, belonging to the oligosaccharide/oligonucleotide-binding domain superfamily, is widely distributed and conserved in prokaryotes, archaea, and eukaryotes. Despite the known tendency to aggregation of ribosomal S1 proteins, the tendency of fibrillation by amyloidogenic regions of this family is poorly understood. In this paper, we combined bioinformatics and experimental approaches to study the features of amyloidogenic regions in this family of proteins. Bioinformatics tools were used to assess the propensity for amyloidogenesis on the example of 1331 sequences of ribosomal S1 protein and to identify such regions in various structural domains. We showed that the fraction of amyloidogenic regions for the full-size proteins decreases with increasing protein size. Within individual domains amyloidogenic regions are more often predicted in the C-and N-terminal parts. For the selected and synthesized 11 amyloidogenic peptides from the Escherichia coli and Thermus thermophilus ribosomal S1 proteins, we showed their ability to form amyloid-like fibrils by electron microscopy.

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“…To gain a better understanding of in vivo protein aggregation and develop an approach to its regulation in the cell, it is necessary to reveal the features of aggregation under conditions close to physiological ones. Currently, such studies are not common, and the data offered in the literature are insufficient to characterize aggregate formation by structured proteins (12,13,(34)(35)(36)(37)(38). Therefore, our goal was to reveal what factors affect amyloidogenicity of a globular protein under nondenaturing conditions.…”

Section: Introductionmentioning

confidence: 99%

sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability

Katina

Balobanov

Ilyina

et al. 2017

Biophysical Journal

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Investigation of the molecular mechanisms underlying amyloid-related human diseases attracts close attention. These diseases, the number of which currently is above 40, are characterized by formation of peptide or protein aggregates containing a cross-β structure. Most of the amyloidogenesis mechanisms described so far are based on experimental studies of aggregation of short peptides, intrinsically disordered proteins, or proteins under denaturing conditions, and studies of amyloid aggregate formations by structured globular proteins under conditions close to physiological ones are still in the initial stage. We investigated the effect of amino acid substitutions on propensity of the completely helical protein sperm whale apomyoglobin (sw ApoMb) for amyloid formation from its structured state in the absence of denaturing agents. Stability and aggregation of mutated sw ApoMb were studied using circular dichroism, Fourier transform infrared spectroscopy, x-ray diffraction, native electrophoresis, and electron microscopy techniques. Here, we demonstrate that stability of the protein native state determines both protein aggregation propensity and structural peculiarities of formed aggregates. Specifically, structurally stable mutants show low aggregation propensity and moderately destabilized sw ApoMb variants form amyloids, whereas their strongly destabilized mutants form both amyloids and nonamyloid aggregates.

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Apomyoglobin mutants with single point mutations at Val10 can form amyloid structures at permissive temperature

Cited by 11 publications

References 37 publications

Kinetics of Mutant Apomyoglobin Association

Kinetics of Mutant Apomyoglobin Association

Investigation of Fibrillation by Amyloidogenic Regions of the Ribosomal S1 Proteins

sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability

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