Effect of Trehalose on Oligomeric State and Anti-Aggregation Activity of αB-Crystallin

Chebotareva, Natalia A.; Eronina, Tatiana B.; Mikhaylova, Valeriya V.; Roman, Svetlana G.; Tugaeva, Kristina V.; Kurganov, B. I.

doi:10.1134/s0006297922020043

Cited by 6 publications

(3 citation statements)

References 44 publications

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“…The similar stabilization effect of Bet and Tre on thermal aggregation of Ph b was shown by us earlier [ 35 , 36 , 37 , 38 ]. In the current work, we have also investigated the effect of these cosolutes during freeze–thawing of Ph b .…”

Section: Discussionsupporting

confidence: 85%

“…Glycogen phosphorylase b from rabbit skeletal muscle (Ph b ) is a dimeric protein formed by two identical subunits with a molecular weight of 97.4 kDa [ 33 ]. Thermal aggregation of Ph b at 48 °C [ 34 ] and the effects of Tre, Bet [ 35 , 36 , 37 , 38 ], and HPCD [ 29 ] on it were previously studied in detail by our team. It was shown that Tre and Bet effectively protected Ph b from thermal denaturation and aggregation.…”

Section: Introductionmentioning

confidence: 99%

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Effect of Chemical Chaperones on the Stability of Proteins during Heat– or Freeze–Thaw Stress

Borzova

Eronina

Mikhaylova

et al. 2023

IJMS

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The importance of studying the structural stability of proteins is determined by the structure–function relationship. Protein stability is influenced by many factors among which are freeze–thaw and thermal stresses. The effect of trehalose, betaine, sorbitol and 2-hydroxypropyl-β-cyclodextrin (HPCD) on the stability and aggregation of bovine liver glutamate dehydrogenase (GDH) upon heating at 50 °C or freeze–thawing was studied by dynamic light scattering, differential scanning calorimetry, analytical ultracentrifugation and circular dichroism spectroscopy. A freeze–thaw cycle resulted in the complete loss of the secondary and tertiary structure, and aggregation of GDH. All the cosolutes suppressed freeze–thaw- and heat-induced aggregation of GDH and increased the protein thermal stability. The effective concentrations of the cosolutes during freeze–thawing were lower than during heating. Sorbitol exhibited the highest anti-aggregation activity under freeze–thaw stress, whereas the most effective agents stabilizing the tertiary structure of GDH were HPCD and betaine. HPCD and trehalose were the most effective agents suppressing GDH thermal aggregation. All the chemical chaperones stabilized various soluble oligomeric forms of GDH against both types of stress. The data on GDH were compared with the effects of the same cosolutes on glycogen phosphorylase b during thermal and freeze–thaw-induced aggregation. This research can find further application in biotechnology and pharmaceutics.

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Section: Discussionsupporting

confidence: 85%

Section: Introductionmentioning

confidence: 99%

Effect of Chemical Chaperones on the Stability of Proteins during Heat– or Freeze–Thaw Stress

Borzova

Eronina

Mikhaylova

et al. 2023

IJMS

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“…In this work, Bet and Arg affected the stage of Ph b aggregate growth in the presence of αB-Cr. Another chemical chaperone, trehalose, acts on the nucleation stage of thermal aggregation of Ph b in the presence of αB-Cr [ 46 ]. According to our data obtained for αB-Cr and another target protein (UV-irradiated Ph b ), Arg acts on both stages of UV-Ph b aggregation (S3).…”

Section: Discussionmentioning

confidence: 99%

Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b

Eronina

Mikhaylova

Chebotareva

et al. 2022

IJMS

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Protein–protein interactions (PPIs) play an important role in many biological processes in a living cell. Among them chaperone–client interactions are the most important. In this work PPIs of αB-crystallin and glycogen phosphorylase b (Phb) in the presence of betaine (Bet) and arginine (Arg) at 48 °C and ionic strength of 0.15 M were studied using methods of dynamic light scattering, differential scanning calorimetry, and analytical ultracentrifugation. It was shown that Bet enhanced, while Arg reduced both the stability of αB-crystallin and its adsorption capacity (AC0) to the target protein at the stage of aggregate growth. Thus, the anti-aggregation activity of αB-crystallin increased in the presence of Bet and decreased under the influence of Arg, which resulted in inhibition or acceleration of Phb aggregation, respectively. Our data show that chemical chaperones can influence the tertiary and quaternary structure of both the target protein and the protein chaperone. The presence of the substrate protein also affects the quaternary structure of αB-crystallin, causing its disassembly. This is inextricably linked to the anti-aggregation activity of αB-crystallin, which in turn affects its PPI with the target protein. Thus, our studies contribute to understanding the mechanism of interaction between chaperones and proteins.

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Effect of osmolytes and posttranslational modifications on modulating the chaperone function of α-crystallin

Singh,

Krishna,

Gupta

et al. 2024

Progress in Molecular Biology and Translational Science

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Effect of Trehalose on Oligomeric State and Anti-Aggregation Activity of αB-Crystallin

Cited by 6 publications

References 44 publications

Effect of Chemical Chaperones on the Stability of Proteins during Heat– or Freeze–Thaw Stress

Effect of Chemical Chaperones on the Stability of Proteins during Heat– or Freeze–Thaw Stress

Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b

Effect of osmolytes and posttranslational modifications on modulating the chaperone function of α-crystallin

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