Article
Biochemistry & Molecular Biology
Tatiana B. Eronina, Valeriya V. Mikhaylova, Natalia A. Chebotareva, Sergey Y. Kleymenov, Anastasia V. Pivovarova, Boris I. Kurganov
Summary: Chemical chaperones are small molecules that enhance protein stability and folding. They have significant effects on the stability, oligomeric state, and aggregation of muscle glycogen phosphorylase b (Phb).
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Biochemistry & Molecular Biology
Tatiana B. Eronina, Valeriya V. Mikhaylova, Natalia A. Chebotareva, Kristina V. Tugaeva, Boris I. Kurganov
Summary: Protein-protein interactions are important for biological processes, and chemical chaperones can influence the structure of proteins, affecting their interactions with target proteins.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Biochemistry & Molecular Biology
Vera A. Borzova, Tatiana B. Eronina, Valeriya V. Mikhaylova, Svetlana G. Roman, Andrey M. Chernikov, Natalia A. Chebotareva
Summary: The structural stability of proteins is important for understanding their function. Freeze-thaw and thermal stresses can affect protein stability. This study investigated the effects of different compounds on the stability and aggregation of bovine liver glutamate dehydrogenase (GDH) under heat and freeze-thaw conditions. The results showed that the cosolutes enhanced protein stability and suppressed aggregation. The findings of this research have potential applications in biotechnology and pharmaceutics.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Vera A. Borzova, Natalia A. Chebotareva, Nikolai N. Sluchanko, Sergey Yu Kleymenov, Kira A. Markossian, Boris Kurganov
Summary: Chemical chaperones are low-molecular compounds that counteract protein aggregation. The aggregation process of bovine liver glutamate dehydrogenase (GDH) at different temperatures was studied, and the unfolding of the protein was found to be the rate-limiting stage of the overall aggregation process. The anti-aggregation activity of chemical chaperones was quantified, and arginine ethyl ester showed the highest activity.
Article
Biochemistry & Molecular Biology
David L. Brautigan
Summary: Glycogen is a polymerized form of glucose used as an energy reserve in organisms. The synthesis and degradation of glycogen in animals, especially in the liver and skeletal muscle, is regulated by hormones and physiological signals that control the activities of glycogen synthase and glycogen phosphorylase. This article discusses the flash activation of phosphorylase in glycogen particles and suggests that the regulation of phosphatase in glycogen particles may involve hybrids of phosphorylase.
Article
Biochemistry & Molecular Biology
Valeriya V. V. Mikhaylova, Tatiana B. B. Eronina, Natalia A. A. Chebotareva, Boris I. I. Kurganov
Summary: Formation and accumulation of protein aggregates negatively impact cellular processes and protein preparations. The effectiveness of chemical chaperones in preventing protein aggregation depends on the structure and kinetics of the target protein. Betaine (Bet) protected Phb and apo-Phb from aggregation, but accelerated the aggregation of UV-Phb. Lysine (Lys) prevented UV-Phb and apo-Phb aggregation, but increased the rate of Phb aggregation. The study provides insights into the mechanisms of chemical chaperone action on protein structure and aggregation kinetics.
BIOCHEMISTRY-MOSCOW
(2023)
Article
Biochemistry & Molecular Biology
Vera A. Borzova, Andrey M. Chernikov, Valeriya V. Mikhaylova, Boris I. Kurganov
Summary: Chemical chaperones are capable of suppressing protein aggregation at different stages. This study investigates the change in aggregation kinetics of yeast alcohol dehydrogenase in the presence of 2-hydroxypropyl-beta-cyclodextrin. The results show that the addition of the chaperone alters the aggregation kinetics and the order of aggregation with respect to protein.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Multidisciplinary Sciences
Hubert Wyszkowski, Anna Janta, Wiktoria Sztangierska, Igor Obuchowski, Tomasz Chamera, Agnieszka Klosowska, Krzysztof Liberek
Summary: The study investigates the functional differences between two classes of JDPs in yeast during the process of protein disaggregation, highlighting the superior aggregate binding ability of Ydj1 and the recruitment of more Ssa1 molecules to substrates by Sis1, which depends on its specific binding mechanism with Hsp70. These findings suggest that the subspecialization of JDPs during protein reactivation improves the robustness and efficiency of the disaggregation machinery.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2021)
Article
Food Science & Technology
Lovedeep Kaur, Harmandeepsingh Lamsar, Ignacio F. Lopez, Manon Filippi, Dayna Ong Shu Min, Kevin Ah-Sing, Jaspreet Singh
Summary: Grass proteins, abundant and potentially novel sources of plant proteins, were extracted from ryegrass using chemical and enzymatic methods in this study. The physico-chemical and digestion properties of the extracted proteins were found to be significantly influenced by the extraction method, highlighting the importance of selecting an appropriate method for optimal protein functionality in food applications.
Review
Biochemistry & Molecular Biology
Maurizio Brunori
Summary: The process of protein folding is a spontaneous reversible process leading from an ensemble of disordered structures to the ordered functional protein. In addition to the native and denatured states, proteins can also populate a third state called amyloid, which is characteristic of incurable neurodegenerative disorders.
Article
Biochemistry & Molecular Biology
Dionysios D. Neofytos, Aristeidis Papagiannopoulos, Evangelia D. Chrysina, Stergios Pispas
Summary: This study investigated the formation and behavior of complexes between rabbit muscle glycogen phosphorylase b (RMGPb) and cationic polyelectrolytes. The results showed that the interaction between the polyelectrolyte and the enzyme affected the size and density of the complexes, but did not induce any changes to the enzyme's secondary structure. These observations suggest that cationic polyelectrolytes can be used to formulate RMGPb in multifunctional nanostructures, which has potential applications in biotechnology and bioinspired materials development.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Biotechnology & Applied Microbiology
Yu Dan, Jiahui Sun, Shanshan Zhang, Yannan Wu, Shaoming Mao, Guodong Luan, Xuefeng Lu
Summary: This study successfully regulated glycogen content in cyanobacteria by enhancing glycogen degradation, leading to increased sucrose production. These findings provide new insights into cyanobacterial glycogen metabolism engineering and will inspire the development of novel metabolic engineering approaches for efficient photosynthetic biosynthesis.
FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
(2022)
Article
Multidisciplinary Sciences
Kimberly Jia Yi Low, Anandalakshmi Venkatraman, Jodhbir S. Mehta, Konstantin Pervushin
Summary: Protein aggregation and deposition in the form of amyloid fibrils is a characteristic feature of amyloid diseases. While most research focuses on inhibiting amyloid formation, it is equally important to understand the disaggregation mechanisms and their potential therapeutic applications. This review compiles the known mechanisms of amyloid disaggregation and explores the use of disaggregases for treating amyloidosis.
JOURNAL OF ADVANCED RESEARCH
(2022)
Article
Chemistry, Applied
Fen Li, Meng-Meng Wang, Qing-Hua Liu, Zhang-Wen Ma, Jun-Jiao Wang, Zi-Yi Wang, Jia-Wei Tang, Jing-Wen Lyu, Zuo-Bin Zhu, Liang Wang
Summary: This study investigates the important roles of two glycogen degradation enzymes in the structural alterations of glycogen in E. coli. The research concludes that glycogen phosphorylase plays a dominant role in glycogen structural stability control.
CARBOHYDRATE POLYMERS
(2023)
Article
Fisheries
Xiaotong Sun, Hongtao Nie, Xiwu Yan
Summary: This study identified and investigated three novel glycogen metabolism-related proteins in Manila clam, suggesting their potential involvement in innate immunity and important role in immune defense.
Article
Biochemistry & Molecular Biology
Anastasiia D. Gonchar, Galina V. Kopylova, Anastasia M. Kochurova, Valentina Y. Berg, Daniil V. Shchepkin, Natalia A. Koubasova, Andrey K. Tsaturyan, Sergey Y. Kleymenov, Alexander M. Matyushenko, Dmitrii I. Levitsky
Summary: Mutations in the TPM3 gene cause structural changes and impaired functional properties in the gamma gamma-Tpm molecule, shedding light on the molecular mechanism of CFTD development and slow skeletal muscle weakness in this inherited disease.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2021)
Article
Biochemistry & Molecular Biology
Victoria V. Nefedova, Natalia A. Koubassova, Vera A. Borzova, Sergey Y. Kleymenov, Andrey K. Tsaturyan, Alexander M. Matyushenko, Dmitrii Levitsky
Summary: This study investigated the effects of mutations mimicking phosphorylation of Tpm on the structural and functional properties of cardiac Tpm carrying cardiomyopathy-associated mutations. The results showed that these mutations can alter the affinity of Tpm for F-actin, potentially influencing the development of heart diseases.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Biochemistry & Molecular Biology
Marina Marchenko, Victoria Nefedova, Natalia Artemova, Sergey Kleymenov, Dmitrii Levitsky, Alexander Matyushenko
Summary: This study investigates the structural and functional differences of five cytoplasmic Tpm isoforms, revealing that sequence variations in alternatively spliced regions of these isoforms can significantly impact their interaction with actin filaments, thus playing a crucial role in cytoskeleton organization and dynamics.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Marina A. Marchenko, Victoria V. Nefedova, Daria S. Yampolskaya, Vera A. Borzova, Sergey Y. Kleymenov, Salavat R. Nabiev, Larisa V. Nikitina, Alexander M. Matyushenko, Dmitrii I. Levitsky
Summary: This study investigated the properties of five low molecular weight Tpm isoforms and found significant differences in their sequences variations in alternatively spliced regions, which may be important for further research on the organization and dynamics of the cytoskeleton.
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
(2021)
Article
Biochemistry & Molecular Biology
Natalia A. Chebotareva, Tatiana B. Eronina, Valeriya V. Mikhaylova, Svetlana G. Roman, Kristina Tugaeva, Boris Kurganov
Summary: This study investigated the effect of trehalose on the quaternary structure and anti-aggregation activity of alpha B-Cr. The results showed that trehalose affected the nucleation stage of Phb thermal aggregation and increased the adsorption capacity of alpha B-Cr during the aggregation process. Additionally, trehalose stabilized the dimeric form of Phb and enhanced the interaction between alpha B-Cr and the target protein.
BIOCHEMISTRY-MOSCOW
(2022)
Article
Biochemistry & Molecular Biology
Vera A. Borzova, Natalia A. Chebotareva, Nikolai N. Sluchanko, Sergey Yu Kleymenov, Kira A. Markossian, Boris Kurganov
Summary: Chemical chaperones are low-molecular compounds that counteract protein aggregation. The aggregation process of bovine liver glutamate dehydrogenase (GDH) at different temperatures was studied, and the unfolding of the protein was found to be the rate-limiting stage of the overall aggregation process. The anti-aggregation activity of chemical chaperones was quantified, and arginine ethyl ester showed the highest activity.
Article
Biochemistry & Molecular Biology
Tatiana B. Eronina, Valeriya V. Mikhaylova, Natalia A. Chebotareva, Sergey Y. Kleymenov, Anastasia V. Pivovarova, Boris I. Kurganov
Summary: Chemical chaperones are small molecules that enhance protein stability and folding. They have significant effects on the stability, oligomeric state, and aggregation of muscle glycogen phosphorylase b (Phb).
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Biochemistry & Molecular Biology
Tatiana B. Eronina, Valeriya V. Mikhaylova, Natalia A. Chebotareva, Kristina V. Tugaeva, Boris I. Kurganov
Summary: Protein-protein interactions are important for biological processes, and chemical chaperones can influence the structure of proteins, affecting their interactions with target proteins.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Biochemistry & Molecular Biology
Andrey K. Tsaturyan, Elena V. Zaklyazminskaya, Margarita E. Polyak, Galina V. Kopylova, Daniil V. Shchepkin, Anastasia M. Kochurova, Anastasiia D. Gonchar, Sergey Y. Kleymenov, Natalia A. Koubasova, Sergey Y. Bershitsky, Alexander M. Matyushenko, Dmitrii I. Levitsky
Summary: The study identified a new variant in the TPM1 gene, which is associated with HCM. The variant increased the thermal stability of the Tpm molecule and its affinity for F-actin was unaffected. However, it increased the Ca2+ sensitivity of filament sliding and impaired its inhibition at low Ca2+ concentration.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Vera A. Borzova, Svetlana G. Roman, Anastasiya V. Pivovarova, Natalia A. Chebotareva
Summary: Intracellular proteins aggregation can be enhanced under stress. Heat-shock proteins (HSPs) and accumulation of osmolytes are cellular protective mechanisms. The antiaggregation activity of HSPB5 can be affected by crowding agents and osmolytes, and different additives can either improve or impair its activity against different protein targets.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Biochemistry & Molecular Biology
Galina V. V. Kopylova, Anastasia M. M. Kochurova, Daria S. S. Yampolskaya, Victoria V. V. Nefedova, Andrey K. K. Tsaturyan, Natalia A. A. Koubassova, Sergey Y. Y. Kleymenov, Dmitrii I. I. Levitsky, Sergey Y. Y. Bershitsky, Alexander M. M. Matyushenko, Daniil V. V. Shchepkin
Summary: The TPM1 gene expresses two isoforms of tropomyosin (Tpm) in the myocardium, alpha (aTpm; Tpm 1.1) and kappa (?Tpm; Tpm 1.2), with ?Tpm being the result of alternative splicing. In this study, the structural features and regulatory function of ?Tpm in the atrial and ventricular myocardium were investigated using an in vitro motility assay. The formation of a?Tpm heterodimer was found to be thermodynamically favorable, indicating that ?Tpm most likely exists as a?Tpm heterodimer in the myocardium.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Alexander M. Matyushenko, Victoria V. Nefedova, Anastasia M. Kochurova, Galina V. Kopylova, Natalia A. Koubassova, Anna G. Shestak, Daria S. Yampolskaya, Daniil V. Shchepkin, Sergey Y. Kleymenov, Natalia S. Ryabkova, Ivan A. Katrukha, Sergey Y. Bershitsky, Elena V. Zaklyazminskaya, Andrey K. Tsaturyan, Dmitrii I. Levitsky
Summary: We characterized a novel genetic variant c.292G > A (p.E98K) in the TPM1 gene encoding cardiac tropomyosin 1.1 isoform (Tpm1.1), which is associated with complex cardiomyopathy, conduction dysfunction, and neuromuscular involvement. We found that the E98K substitution in Tpm1.1 significantly destabilizes its structure and impairs its regulatory properties. This study provides insights into the mechanism by which the E98K Tpm mutation affects myocardial function and relaxation.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
A. A. Pometun, P. D. Parshin, N. P. Galanicheva, L. A. Shaposhnikov, D. L. Atroshenko, E. Pometun, V. V. Burmakin, S. Yu Kleymenov, S. S. Savin, V. Tishkov
Summary: A mutant formate dehydrogenase (PseFDH) from Pseudomonas sp. 101 bacterium with improved thermal stability has been generated through single-point amino acid replacements. The mutant with E170D substitution exhibits increased thermal stability compared to the starting mutant and the wild-type enzyme.