Publications by authors named "Ali A Moosavi-Movahedi"

Neurodegenerative diseases, particularly Alzheimer's disease and Parkinson's disease, present formidable challenges in modern medicine due to their complex pathologies and the absence of curative treatments. Despite advances in symptomatic management, early diagnosis remains essential for mitigating disease progression and improving patient outcomes. Traditional diagnostic methods, such as MRI, PET, and cerebrospinal fluid biomarker analysis, are often inadequate for the early detection of these diseases.

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Parkinson's disease (PD), a chronic and common neurodegenerative disease, is characterized by the progressive loss of dopaminergic neurons in the dense part of the substantia nigra and abnormal aggregation of alpha-synuclein. Type 2 diabetes mellitus (T2DM) is a metabolic disease characterized by chronic insulin resistance and deficiency in insulin secretion. Extensive evidence has confirmed shared pathogenic mechanisms underlying PD and T2DM, such as oxidative stress caused by insulin resistance, mitochondrial dysfunction, inflammation, and disorders of energy metabolism.

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Human serum albumin (HSA), a crucial plasma protein, plays a significant role in drug interactions within the bloodstream, bearing considerable clinical relevance. Bortezomib (BTZ) is a potent anti-cancer drug for multiple myeloma (MM) and mantle cell lymphoma (MC). The mechanism of BTZ transfer in the blood remains undetermined.

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Article Synopsis
  • Triple-negative breast cancer (TNBC) is difficult to treat due to its aggressive characteristics, leading researchers to explore innovative delivery methods for medications.
  • Human serum albumin (HSA) was used to encapsulate Lapatinib (LAP), a drug effective against TNBC, improving its solubility and targeting capabilities in tumor environments.
  • The combination of HSA-LAP with a VEGFR-targeting peptide (VGB3) significantly enhanced anti-cancer effects, including better tumor inhibition and survival rates in animal models, indicating a compelling strategy for TNBC treatment.
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  • Researchers produced electrospun mats featuring coelomic fluid (CF) from earthworms integrated with chitosan (Chs) and polyvinyl alcohol (PVA) for potential wound dressing applications.
  • The CF-infused dressings demonstrated significantly better antibacterial, antioxidant, and cell viability properties compared to control samples without CF.
  • In vivo tests on Wistar albino rats showed that the Chs/PVA/CF dressings enhanced wound healing and re-epithelialization, indicating their effectiveness as a wound dressing material.
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  • Luteolin possesses anti-inflammatory, antioxidant, and antitumor properties, making its detection crucial in drug development and functional foods.
  • A new method was developed using a modified glassy carbon electrode that combines horseradish peroxidase with metal-organic frameworks and carbon nanotubes to enhance selectivity and conductivity for luteolin detection.
  • The resulting biosensor demonstrated a linear detection range of 1.0 × 10 to 6.0 μM, a detection limit of 25.3 nM, and effective long-term stability, successfully detecting luteolin in various vegetables like carrots, celery, and cauliflower.
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This research focused on utilizing periodic mesoporous organosilica with imidazolium framework (PMO-IL), to immobilize a metagenome-sourced protease (PersiProtease1), thereby enhancing its functional efficiency and catalytic effectiveness in processing primary proteins found in tannery wastewater. The successful immobilization of enzyme was confirmed through the use of N adsorption-desorption experiment, XRD, FTIR, TEM, FESEM, EDS and elemental analytical techniques. The immobilized enzyme exhibited greater stability in the presence of various metal ions and inhibitors compared to its free form.

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Growing epidemiological evidence indicates an association between obesity, type 2 diabetes, and certain cancers, suggesting the existence of common underlying mechanisms in these diseases. Frequent hyperglycemias in type 2 diabetes promote pro-inflammatory responses and stimulate intracellular metabolic flux which rewires signaling pathways and influences the onset and advancement of different types of cancers. Here, we review the provocative impact of hyperglycemia on a subset of interconnected signalling pathways that regulate (i) cell growth and survival, (ii) metabolism adjustments, (iii) protein function modulation in response to nutrient availability (iv) and cell fate and proliferation and which are driven respectively by PI3K (Phosphoinositide 3-kinase), AMPK (AMP-activated protein kinase), O-GlcNAc (O-linked N-acetylglucosamine) and Wnt/β-catenin.

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Catalase (CAT), a ubiquitous enzyme in all oxygen-exposed organisms, effectively decomposes hydrogen peroxide (HO), a harmful by-product, into water and oxygen, mitigating oxidative stress and cellular damage, safeguarding cellular organelles and tissues. Therefore, CAT plays a crucial role in maintaining cellular homeostasis and function. Owing to its pivotal role, CAT has garnered considerable interest.

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The importance of amyloid nanofibrils made from food proteins is rising in diverse fields, such as biomedicine and food science. These protein nanofibrils (PNFs) serve as versatile and sustainable building blocks for biomaterials, characterized by their high β-sheet content and an ordered hydrogen bond network. These properties offer both stability and flexibility, along with an extreme aspect ratio and reactive functional groups.

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Designing and synthesizing one-dimensional porous Pt nanocrystals with unique optical, electrocatalytic, and theranostic properties are gaining lots of attention, especially to overcome the challenges of tumor recurrence and resistance to platinum-based chemotherapy. Herein, we represented an interesting report of a one-step and facile strategy for synthesizing multifunctional one-dimensional (1D) porous Pt nanoribbons (PtNRBs) with highly efficient therapeutic effects on cancer cells based on inherent electrocatalytic activity. The critical point in the formation of luminescent porous PtNRBs was the use of human hemoglobin (Hb) as a shape-regulating, stabilizing, and reducing agent with facet-specific domains on which fluorescent platinum nanoclusters at first are aggregated by aggregation-induced emission phenomena (AIE) and then crystallized into contact and penetration twins, as intermediate products, followed by shaping of the final luminescent porous ribbon nanomaterials, owing to oriented attachment association the Ostwald ripening mechanism.

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Bacteriophage endolysins are potential alternatives to conventional antibiotics for treating multidrug-resistant gram-negative bacterial infections. However, their structure-function relationships are poorly understood, hindering their optimization and application. In this study, we focused on the individual functionality of the C-terminal muramidase domain of Gp127, a modular endolysin from E.

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A revolution in chemical biology occurred with the introduction of click chemistry. Click chemistry plays an important role in protein chemistry modifications, providing specific, sensitive, rapid, and easy-to-handle methods. Under physiological conditions, click chemistry often overlaps with bioorthogonal chemistry, defined as reactions that occur rapidly and selectively without interfering with biological processes.

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The substitution of leucine to proline at position 39 (p.P39L) in human αB-crystallin (αB-Cry) has been associated with conflicting interpretations of pathogenicity in cataracts and cardiomyopathy. This study aimed to investigate the effects of the p.

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In pulmonary inflammation diseases, like COVID-19, lung involvement and inflammation determine the treatment regime. Respiratory inflammation is typically arisen due to the cytokine storm and the leakage of the vessels for immune cells recruitment. Currently, such a situation is detected by the clinical judgment of a specialist or precisely by a chest CT scan.

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To date, several pathogenic mutations have been identified in the primary structure of human α-Crystallin, frequently involving the substitution of arginine with a different amino acid. These mutations can lead to the incidence of cataracts and myopathy. Recently, an important cataract-associated mutation has been reported in the functional α-Crystallin domain (ACD) of human αB-Crystallin protein, where arginine 107 (R107) is replaced by a leucine.

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αB-Crystallin (αB-Cry) is a small heat shock protein known for its protective role, with an adaptable structure that responds to environmental changes through oligomeric dynamics. Cu(II) ions are crucial for cellular processes but excessive amounts are linked to diseases like cataracts and neurodegeneration. This study investigated how optimal and detrimental Cu(II) concentrations affect αB-Cry oligomers and their chaperone activity, within the potassium-regulated ionic-strength environment.

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In the present study, we investigated the effects of N-homocysteine thiolactone (tHcy) modification on expressed and purified tau protein and the synthesized VQIVYK target peptide. The modified constructs were subjected to comprehensive validation using various methodologies, including mass spectrometry. Subsequently, in vivo, in vitro, and in silico characterizations were performed under both reducing and non-reducing conditions, as well as in the presence and absence of heparin as a cofactor.

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Tau cleavage has been shown to have a significant effect on protein aggregation. Tau truncation results in the formation of aggregation-prone fragments leading to toxic aggregates and also causes the formation of harmful fragments that do not aggregate. Thus, targeting proteolysis of tau would be beneficial for the development of therapeutics for Alzheimer's disease and related tauopathies.

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αB-crystallin, a member of the small heat shock protein (sHSP) family, is expressed in diverse tissues, including the eyes, brain, muscles, and heart. This protein plays a crucial role in maintaining eye lens transparency and exhibits holdase chaperone and anti-apoptotic activities. Therefore, structural and functional changes caused by genetic mutations in this protein may contribute to the development of disorders like cataract and cardiomyopathy.

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Angiotensin-converting enzyme 2 (ACE2) has a specific interaction with the coronavirus spike protein, enabling its entry into human cells. This membrane enzyme converts angiotensin II into angiotensin 1-7, which has an essential role in protecting the heart and improving lung function. Many therapeutic properties have been attributed to the human recombinant ACE2 (hrACE2), especially in combating complications related to diabetes mellitus and hypertension, as well as, preventing the coronavirus from entering the target tissues.

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The transfusion of donor red blood cells (RBCs) is seriously hampered by important drawbacks that include limited availability and portability, the requirement of being stored in refrigerated conditions, a short shelf life or the need for RBC group typing and crossmatching. Thus, hemoglobin (Hb)-based oxygen (O) carriers (HBOCs) which make use of the main component of RBCs and the responsible protein for O transport, hold a lot of promise in modern transfusion and emergency medicine. Despite the great progress achieved, it is still difficult to create HBOCs with a high Hb content to attain the high O demands of our body.

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Advanced glycation end products are the most important species of glycation pathway, and cause disorders such as oxidative stress and diabetes. Sulfonamide compounds, which are generally known as widespread inhibitors, are potential agents used in different drug products, which can readily enter biological matrices. In the present work, the structure and activity of human carbonic anhydrase II studied in the presence of glucose as well as four sulfonamide agents from different views.

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Article Synopsis
  • * The study focused on this mutation's effects on αB-Cry, using laboratory techniques to generate, express, and purify both the mutant and normal proteins for comparison.
  • * Findings revealed that the p.D109G mutation led to significant structural changes, increased chaperone activity, reduced stability, and a higher likelihood of forming damaging amyloid aggregates, which can disrupt normal muscle cell function.
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Synopsis of recent research by authors named "Ali A Moosavi-Movahedi"

  • - Ali A Moosavi-Movahedi's research primarily focuses on the interactions and structural dynamics of proteins, particularly in relation to modifications such as glycation and the effects of small molecules, which have implications in fields such as biochemistry and pharmacology.
  • - His findings reveal insights into the competitive effects of drugs like acetazolamide on carbonic anhydrase, the electrochemical properties of caffeic acid, and the structural changes in proteins such as human serum albumin due to modification, providing a deeper understanding of biochemical pathways relevant to diabetes and enzyme activity.
  • - The research also explores innovative methods for the quantification of biological substances, including a bromide-modified silver electrode for hemoglobin measurement, emphasizing the significance of electrostatic interactions and environmental factors in protein aggregation and stability.