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Analysis of the Secondary Structure of Chromatin Linker Proteins HMGB1 and H1 and their Complexes 染色质连接蛋白 HMGB1 和 H1 及其复合物的二级结构分析
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S0006350923050081
E. V. Chikhirzhina, A. M. Polyanichko
{"title":"Analysis of the Secondary Structure of Chromatin Linker Proteins HMGB1 and H1 and their Complexes","authors":"E. V. Chikhirzhina,&nbsp;A. M. Polyanichko","doi":"10.1134/S0006350923050081","DOIUrl":"10.1134/S0006350923050081","url":null,"abstract":"<p>The nonhistone chromosomal protein HMGB1 and histone H1 are chromatin linker proteins. The functions of linker proteins are closely related to their conformational state. The structure of proteins that play a key role in the formation of higher levels of chromatin structural organization is being actively studied. In this study, a comparative analysis of the secondary structure of the linker histone H1 and the nonhistone protein HMGB1 was carried out. Using circular dichroism in the UV region and FTIR spectroscopy, it was shown that positively charged histone H1 binds to the C-terminal fragment of HMGB1, stabilizing the resulting complex and inducing the formation of additional α-helical regions in both proteins.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"725 - 730"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140884783","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The Complex System of the Mouse Brain: Selection for Successful Solution of a Cognitive Test 小鼠大脑的复杂系统：成功完成认知测试的选择
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S0006350923050238
I. I. Poletaeva, O. V. Perepelkina, Z. A. Zorina
{"title":"The Complex System of the Mouse Brain: Selection for Successful Solution of a Cognitive Test","authors":"I. I. Poletaeva,&nbsp;O. V. Perepelkina,&nbsp;Z. A. Zorina","doi":"10.1134/S0006350923050238","DOIUrl":"10.1134/S0006350923050238","url":null,"abstract":"<p>This study provides a review of experimental research on selection in mice, which yielded positive results. The selection of mice was high (the task required mice to understand that an object that has become invisible still exists and can be found) and poor performance occurred in a cognitive test. The results we obtained revealed better short term memory in mice selected for high performance scores and that these mice also had higher performance in tests for novelty and attention. This suggests that differences between the mice used in the experiment are associated not only with cognitive abilities in tests, but also with more pronounced “executive functions.”</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"864 - 873"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140884494","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Deep Hypothermia Inverts the Inotropic Effect of Isoproterenol in the Rat Myocardium 深度低温会削弱异丙肾上腺素对大鼠心肌的肌力作用
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S0006350923050251
C. V. Samodurova, F. V. Turin, A. S. Averin
{"title":"Deep Hypothermia Inverts the Inotropic Effect of Isoproterenol in the Rat Myocardium","authors":"C. V. Samodurova,&nbsp;F. V. Turin,&nbsp;A. S. Averin","doi":"10.1134/S0006350923050251","DOIUrl":"10.1134/S0006350923050251","url":null,"abstract":"<p>The effects of the β-adrenergic receptor agonist isoproterenol on the contractile activity of the papillary muscle of the rat heart right ventricle were studied both at a temperature close to physiological (30°C) and under conditions of deep hypothermia (10°C). Isoproterenol had a pronounced positive inotropic effect at 30°C, the contraction force increased from 1.2 ± 0.1 mN in the control to 2.4 ± 0.4 mN after the addition of the agonist and there was a significant acceleration of the time parameters of contraction, that is, the time to reach the maximum contraction decreased from 101 ± 6 ms to 85 ± 4 ms; the relaxation time decreased by 50% from 55 ± 3 ms to 36 ± 1 ms. Under hypothermic conditions, isoproterenol caused a powerful negative inotropic effect, reducing the contraction force from 2.2 ± 0.4 mN to 1.2 ± 0.4 mN. The tendency to accelerate contraction persisted as at 30°C: the time to reach the maximum contraction decreased from 717 ± 52 ms to 624 ± 50 ms, and the relaxation time decreased by 50% from 667 ± 86 ms to 450 ± 40 ms. Thus, under conditions of deep hypothermia at 10°C, the direction of the inotropic response to isoproterenol changed from positive to negative, while the lusitropic effect remained negative.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"831 - 835"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140073131","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Mechanism of Action of the Low-Frequency Electromagnetic Field on Aqueous Solutions of Biopolymers 低频电磁场对生物聚合物水溶液的作用机制
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S0006350923050299
E. E. Tekutskaya, G. P. Ilchenko, M. G. Baryshev
{"title":"Mechanism of Action of the Low-Frequency Electromagnetic Field on Aqueous Solutions of Biopolymers","authors":"E. E. Tekutskaya,&nbsp;G. P. Ilchenko,&nbsp;M. G. Baryshev","doi":"10.1134/S0006350923050299","DOIUrl":"10.1134/S0006350923050299","url":null,"abstract":"<p>This paper presents the transformation mechanism of a signal from the magnetic component of a low-frequency electromagnetic field with extremely low energy into a chemical and biochemical response in aqueous solutions of nucleic acids and proteins. The developed theoretical model shows that oxidative DNA damage and conformational transitions in proteins are based on a universal mechanism for changing the amount of the most long-lived form, hydrogen peroxide, in a chemical oscillator of mutual transformations of reactive oxygen species under a low-intensity electromagnetic field. It has been experimentally found that the content of hydrogen peroxide in solutions of biopolymers resonantly depends on the frequency of the applied field. Conformational changes in proteins are accompanied by increasing accessibility and activity of the nucleophilic centers, which are potential targets for reactive oxygen species. Complete unfolding and denaturation of the protein amino-acid chain in a low-frequency electromagnetic field did not occur. It has been shown that the enhanced formation of hydrogen peroxide at 3 and 50 Hz leads to oxidative modification of nitrogenous bases in DNA.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"738 - 746"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140884725","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Patterns of Adaptational Changes in Leukocytes and Platelets of Yakutian Ground Squirrels during the Pre-Hibernation Period in Autumn 秋季冬眠前期雅库特地松鼠白细胞和血小板的适应性变化模式
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S0006350923050305
P. O. Teplova, N. P. Komelina, K. I. Lizorkina, N. M. Zakharova
{"title":"Patterns of Adaptational Changes in Leukocytes and Platelets of Yakutian Ground Squirrels during the Pre-Hibernation Period in Autumn","authors":"P. O. Teplova,&nbsp;N. P. Komelina,&nbsp;K. I. Lizorkina,&nbsp;N. M. Zakharova","doi":"10.1134/S0006350923050305","DOIUrl":"10.1134/S0006350923050305","url":null,"abstract":"<p>Previously, it has been shown that a series of physiological and biochemical changes occur in Yakutian long-tailed ground squirrels during autumn (the pre-hibernation period), involving the brain, heart, skeletal muscles, and other organs. This study was conducted to analyze the composition of peripheral blood cells obtained from Yakutian ground squirrels in autumn. For the first time, an increase in the total number of leukocytes, particularly granulocytes, and a decrease in the number of lymphocytes were observed when compared with samples obtained in summer; a leukogram shift from the lymphocytic to the granulocytic fraction was revealed. Significant increase in platelet counts and thrombocrit with preservation of the percentage ratio of mature and young cell fractions was shown. To date, information on the cellular components of blood during the autumn season when hibernators prepare for winter months of hibernation remains scarce. Nonetheless, the results of our study indicate that very significant adaptive changes occur in leukocytes and platelets of ground squirrels in this period. Possible causes of these changes are discussed.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"760 - 764"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140071732","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
In Silico Study of Solvation Effects in Solutions of Biomolecules: Possibilities of an Approach Based on the 3D-Distribution of Solvent Atomic Density 生物大分子溶液溶解效应的硅学研究：基于溶剂原子密度三维分布的方法的可能性
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S0006350923050123
S. E. Kruchinin, M. V. Fedotova, E. E. Kislinskaya, G. N. Chuev
{"title":"In Silico Study of Solvation Effects in Solutions of Biomolecules: Possibilities of an Approach Based on the 3D-Distribution of Solvent Atomic Density","authors":"S. E. Kruchinin,&nbsp;M. V. Fedotova,&nbsp;E. E. Kislinskaya,&nbsp;G. N. Chuev","doi":"10.1134/S0006350923050123","DOIUrl":"10.1134/S0006350923050123","url":null,"abstract":"<p>Biomolecular solvation plays a key role in nature. Biological activity and target functions of molecules depend on the features of the process. However, hydration of biomolecules is an intricate problem in both experimental research and computer simulations. The possibilities of the non-empirical 3D-SDFT/3D-RISM approach based on the 3D-distribution of the solvent atomic density to study the features of biomolecule hydration were demonstrated with examples of a number of amino acids (Gly-ZW, L-Ala-ZW, L-Val-ZW, and L-Pro-ZW), two model proteins (bovine pancreatic trypsin inhibitor (BPTI)) and protein tyrosine phosphatase 1B (PTP1B)), and PTP1B complexes with inhibitors. The results showed that using this approach it is possible to simultaneously obtain a detailed and holistic description of the hydration shell structure of biomolecules.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"681 - 692"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140073127","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Evaluation of the Efficiency of Intersystem Crossing to a Triplet State of Fullerene in Complexes with Amino Acids 评估富勒烯与氨基酸复合物的三重态系统间交叉效率
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S000635092305007X
A. S. Buchelnikov, P. A. Sokolov, R. R. Ramasanoff
{"title":"Evaluation of the Efficiency of Intersystem Crossing to a Triplet State of Fullerene in Complexes with Amino Acids","authors":"A. S. Buchelnikov,&nbsp;P. A. Sokolov,&nbsp;R. R. Ramasanoff","doi":"10.1134/S000635092305007X","DOIUrl":"10.1134/S000635092305007X","url":null,"abstract":"<p>The important photophysical process that determines the efficiency of photosensitizers is saturation of the triplet state through the intersystem crossing during light absorption. We studied the C<sub>60</sub> fullerene complexes with the amino acids (glycine, lysine, methionine, and threonine) as promising photosensitizers. The calculations for all these complexes demonstrate high values of the transition rate constants to the triplet states and a high probability of generating reactive oxygen species upon excitation in visible light. The carboxyl groups of amino acids, which are not involved in electronic excitation, can be used to conjugate photoactive complexes with a tumor-targeting drug delivery system, such as specific DNA aptamers.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"693 - 697"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140076365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The Effect of an Electrochemically Activated Water Solution on Plant Polysaccharides: Phenomenology and Spectrometry 电化学活化水溶液对植物多糖的影响：现象学与光谱学
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S0006350923050226
A. G. Pogorelov, L. G. Ipatova, A. I. Panait, M. A. Pogorelova, A. A. Gulin, V. N. Pogorelova
{"title":"The Effect of an Electrochemically Activated Water Solution on Plant Polysaccharides: Phenomenology and Spectrometry","authors":"A. G. Pogorelov,&nbsp;L. G. Ipatova,&nbsp;A. I. Panait,&nbsp;M. A. Pogorelova,&nbsp;A. A. Gulin,&nbsp;V. N. Pogorelova","doi":"10.1134/S0006350923050226","DOIUrl":"10.1134/S0006350923050226","url":null,"abstract":"<p>Changes in the properties of polysaccharides in an electrochemically activated aqueous solution have been studied using UV-Vis spectrometry, time-of-flight secondary ion mass spectrometry and scanning electron microscopy. It is shown that the studied solutions of polysaccharides of plant origin (agar, soluble starch, and food starch) are subject to modification, the direction of which is determined by the fraction of electrochemically activated solution used (catholyte or anolyte). The identified features may be in demand when developing new ways to control the properties of biological raw materials in food production technology. It was noted that the technology of an electrochemically activated aqueous solution, which has been classified as “green,” can be reproduced on an industrial scale.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"705 - 711"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140071723","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Conformational Features of Beta-Amyloid Peptide 25–35 β-淀粉样肽 25-35 的构象特征
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S0006350923050020
G. A. Agaeva, G. Z. Najafova
{"title":"Conformational Features of Beta-Amyloid Peptide 25–35","authors":"G. A. Agaeva,&nbsp;G. Z. Najafova","doi":"10.1134/S0006350923050020","DOIUrl":"10.1134/S0006350923050020","url":null,"abstract":"<p>Beta-amyloid peptide (Aβ) plays an important role in the mechanism of neurodegeneration in Alzheimer’s disease. A fragment of beta-Aβ(25–35) amyloid peptide with the sequence GSNKGAIIGLM is considered to be the functional domain of the amyloid Aβ peptide responsible for its neurotoxic properties and the biologically active Aβ region. Conformational analysis by the method of molecular mechanics of each peptide segment of the C-terminal part of the peptide revealed a limited number of the most probable conformations and clearly defined the forces stabilizing the structures. The results we obtained showed that the Aβ(25–35) peptide energetically preferentially adopts the a-helical conformation at the C-terminal octapeptide segment. The molecular dynamics method was used to model the intramolecular mobility pattern of the Aβ(25–35) peptide molecule. It is shown that in the low-energy conformations of the Aβ(25–35) peptide, the flexible structures in its N-terminal region were oriented differently with respect to the structures in the C-terminal part.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"712 - 718"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140073043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
A Raman Spectroscopic Study of the Conformation of Flavin Adenine Dinucleotide, a CoEnzyme of D-Amino Acid Oxidase 关于 D-氨基酸氧化酶辅酶黄素腺嘌呤二核苷酸构象的拉曼光谱研究
IF 4.033
Biophysics Pub Date : 2024-03-07 DOI: 10.1134/S0006350923050068
J. V. Bochkova, W. Liu, N. A. Brazhe, A. A. Zhgun, G. V. Maksimov
{"title":"A Raman Spectroscopic Study of the Conformation of Flavin Adenine Dinucleotide, a CoEnzyme of D-Amino Acid Oxidase","authors":"J. V. Bochkova,&nbsp;W. Liu,&nbsp;N. A. Brazhe,&nbsp;A. A. Zhgun,&nbsp;G. V. Maksimov","doi":"10.1134/S0006350923050068","DOIUrl":"10.1134/S0006350923050068","url":null,"abstract":"<p>The spectra of surface-enhanced Raman scattering of D-amino acid oxidase from pig kidney were recorded and analyzed using silver nanoparticles; characteristic spectral parameters of changes in the conformation of the flavinadenine dinucleotide cofactor during activation of the enzyme by D-amino acids were revealed. It was found that the time during which changes in the conformation of the flavinadenine dinucleotide were recorded depended on the substrate specificity of the enzyme: in the presence of D-alanine, this took several seconds, and in the presence of D-serine, minutes.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"719 - 724"},"PeriodicalIF":4.033,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140071731","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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