Maksim I. Sulatsky

ORCID: 0000-0003-4665-3181
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About
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Research Areas
  • Alzheimer's disease research and treatments
  • Prion Diseases and Protein Misfolding
  • Protein Structure and Dynamics
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Enzyme Structure and Function
  • Protein Interaction Studies and Fluorescence Analysis
  • Amino Acid Enzymes and Metabolism
  • Terahertz technology and applications
  • Protein purification and stability
  • Proteins in Food Systems
  • Bacterial Genetics and Biotechnology
  • Enzyme Production and Characterization
  • Phytase and its Applications
  • Trace Elements in Health
  • Aluminum toxicity and tolerance in plants and animals
  • Legume Nitrogen Fixing Symbiosis
  • Biochemical Acid Research Studies
  • Advanced Glycation End Products research
  • Insect and Pesticide Research
  • Olfactory and Sensory Function Studies
  • Biochemical Analysis and Sensing Techniques
  • Parkinson's Disease Mechanisms and Treatments
  • Glycosylation and Glycoproteins Research
  • Cholinesterase and Neurodegenerative Diseases
  • Supramolecular Self-Assembly in Materials

Institute of Cytology
2017-2025

Morpho (United States)
2022

Russian Academy of Sciences
2021

ITMO University
2014-2015

Amyloid fibrils cause organ and tissue dysfunction in numerous severe diseases. Despite the prevalence severity of amyloidoses, there is still no effective safe anti-amyloid therapy. This study investigates impact cysteine protease cathepsin B (CTSB) on amyloids associated with Alzheimer's Parkinson's diseases, hemodialysis, lysozyme amyloidosis. We analyzed effect CTSB size, structure, proteotoxicity amyloid formed from alpha-synuclein, abeta peptide (1-42), insulin, using a combination...

10.1038/s41420-025-02343-w article EN cc-by Cell Death Discovery 2025-02-15

ABSTRACT Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer's, Parkinson's, prion etc. However, possible effect these on is not well understood. In this work, we investigated photophysical characteristics, structure, morphology mature formed from two model proteins, insulin lysozyme, presence ThT ANS. It turned out ANS affects secondary...

10.1080/19336896.2020.1720487 article EN cc-by Prion 2020-01-01

Amyloids are protein aggregates with a highly ordered spatial structure giving them unique physicochemical properties. Different amyloids not only participate in the development of numerous incurable diseases but control vital functions archaea, bacteria and eukarya. Plants poorly studied systematic group field amyloid biology. Amyloid properties have yet been demonstrated for plant proteins under native conditions vivo. Here we show that seeds garden pea Pisum sativum L. contain...

10.1371/journal.pbio.3000564 article EN cc-by PLoS Biology 2020-07-23

Abstract Extrapulmonary tuberculosis with a renal involvement can be manifestation of disseminated infection that requires therapeutic intervention, particularly decrease in efficacy conventional regimens. In the present study, we investigated potency mesenchymal stem cell-derived extracellular vesicles (MSC-EVs) complex anti-tuberculosis treatment (ATT). A rabbit model (rTB) was constructed by injecting standard strain Mycobacterium H37Rv into cortical layer kidney parenchyma. Isolated...

10.1038/s41598-024-54992-z article EN cc-by Scientific Reports 2024-02-24

In this work, α-synuclein amyloid fibrils-the formation of which is a biomarker Parkinson's disease-were investigated using the fluorescent probe thioflavin T (ThT). The experimental conditions protein fibrillogenesis were chosen so that sufficient number continuous measurements could be performed to characterize and analyze all stages process. reproducibility structure obtained aggregates (which critical point for further investigation) proven wide range physical-chemical methods. For...

10.3390/ijms19092486 article EN International Journal of Molecular Sciences 2018-08-23

Background: The most obvious manifestation of amyloidoses is the accumulation amyloid fibrils as plaques in tissues and organs, which always leads to a noticeable deterioration patients' condition main marker disease. For this reason, early diagnosis amyloidosis difficult, inhibition fibrillogenesis, when mature amyloids are already accumulated large quantities, ineffective. A new direction for treatment development approaches aimed at degradation fibrils. In present work, we investigated...

10.3389/fmolb.2023.1208059 article EN cc-by Frontiers in Molecular Biosciences 2023-06-12

Outer membrane proteins (Omps) of Gram-negative bacteria represent porins involved in a wide range virulence- and pathogenesis-related cellular processes, including transport, adhesion, penetration, the colonization host tissues. Most outer share specific spatial structure called β-barrel that provides their structural integrity within lipid bilayer. Recent data suggest from several bacterial species are able to adopt amyloid state alternative structure. Amyloids protein fibrils with cross-β...

10.3390/ijms242115522 article EN International Journal of Molecular Sciences 2023-10-24

Ordered protein aggregates, amyloid fibrils, form toxic plaques in the human body amyloidosis and neurodegenerative diseases provide adaptive benefits to pathogens reduce nutritional value of legumes. To identify amyloidogenic properties proteins study processes fibril formation degradation, cationic dye thioflavin T (ThT) is most commonly used. However, its use acidic environments that induce vitro can sometimes lead misinterpretation experimental results due electrostatic repulsion. In...

10.1021/acs.analchem.3c05118 article EN Analytical Chemistry 2024-01-25

The colloidal long-storage stability of nanosized drugs is a crucial factor for pharmacology, as they require much time robust estimation. application bioavailable magnetic nanosuspensions in theranostics limited by incomplete information about their the internal media human organisms. A method accelerated temperature stress “aging” suspensions proposed rapid assessment and prediction over iron oxide stabilized albumin HSA. Colloidal assessed using dynamic light scattering (DLS),...

10.3390/nano15070475 article EN cc-by Nanomaterials 2025-03-21

Amyloids represent protein fibrils with a highly ordered spatial structure, which not only cause dozens of incurable human and animal diseases but also play vital biological roles in Archaea, Bacteria, Eukarya. Despite the fact that association bacterial amyloids microbial pathogenesis infectious is well known, there lack information concerning symbiotic bacteria. In this study, using previously developed proteomic method for screening identification (PSIA), we identified amyloidogenic...

10.3390/biom9110694 article EN cc-by Biomolecules 2019-11-04

Proteolytic enzymes are known to be involved in the formation and degradation of various monomeric proteins, but effect proteases on ordered protein aggregates, amyloid fibrils, which considered extremely stable, remains poorly understood. In this work we study resistance proteolytic lysozyme fibrils with two different types morphology beta-2-microglobulun amyloids. We showed that enzyme pancreas, trypsin, induced mechanism process was qualitatively same for all investigated At time, found a...

10.3390/ijms22094828 article EN International Journal of Molecular Sciences 2021-05-02

The relative abundance of two main Abeta-peptide types with different lengths, Aβ40 and Aβ42, determines the severity Alzheimer's disease progression. However, factors responsible for behavior patterns these peptides in amyloidogenesis process remain unknown. In this comprehensive study, new evidence on Aβ42 amyloid polymorphism was obtained using a wide range experimental approaches, including custom-designed approaches. We have first time determined number modes thioflavin T (ThT) binding...

10.3390/ijms23105513 article EN International Journal of Molecular Sciences 2022-05-15

The persistence of high concentrations beta-2-microglobulin (β2M) in the blood patients with acute renal failure leads to development dialysis-related amyloidosis. This disease manifests deposition amyloid fibrils formed from various forms β2M tissues and biological fluids patients. In this paper, full-length (β2m) its variants that lack 6 10 N-terminal amino acids protein polypeptide chain (ΔN6β2m ΔN10β2m, respectively) were probed by using fluorescent dye thioflavin T (ThT). For aim,...

10.3390/ijms19092762 article EN International Journal of Molecular Sciences 2018-09-14

The observed differences in the structure of native tissue and formed vitro cause loss functional activity cells cultured vitro. lack fundamental knowledge about protein mechanism interactions limits ability to effectively create tissue. Collagen is able spontaneously assemble into fibrils vitro, but vivo, other proteins, for example fibronectin, have a noticeable effect on this process. molecular or fibrillar collagen plays an equally important role. Therefore, we studied interaction with...

10.3390/ijms232012577 article EN International Journal of Molecular Sciences 2022-10-20

Fluorescent dye trans-2-[4-(dimethylamino)styryl]-3-ethyl-1,3-benzothiazolium perchlorate (DMASEBT) is a relatively recently synthesized probe for detection of amyloid fibrils accumulating in the organs and tissues patients with wide range serious incurable diseases. DMASEBT was developed as an alternative its widely used analogue thioflavin T (ThT), which "gold standard" study. Our results show similarity both dyes binding to allow one propose mechanism such probes interaction some types...

10.1021/acs.analchem.8b05737 article EN Analytical Chemistry 2019-01-23

Thioflavin T (ThT) is a widely used fluorescent probe of amyloid fibrils, which accompanies many serious neurodegenerative and other diseases. Until recently, examinations processes fibril formation in vitro were conducted solutions whose properties significantly different from those found inside the densely packed cells. Such crowded cellular milieu typically simulated using concentrated inert polymers, do not usually interact with proteins. However, these crowding agents can have direct...

10.1155/2017/2365746 article EN cc-by Journal of Spectroscopy 2017-01-01

Given the ability of molecular chaperones and chaperone-like proteins to inhibit formation pathological amyloid fibrils, chaperone-based therapy amyloidosis has recently been proposed. However, since these diseases are often diagnosed at stages when a large amount amyloids is already accumulated in patient’s body, this work we pay attention undeservedly poorly studied problem chaperone proteins’ effect on mature fibrils. We showed that heat shock protein alpha-B-crystallin, which capable...

10.3390/ijms21207659 article EN International Journal of Molecular Sciences 2020-10-16
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