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  1. Article ; Online: NSAID targets SIRT3 to trigger mitochondrial dysfunction and gastric cancer cell death.

    Debsharma, Subhashis / Pramanik, Saikat / Bindu, Samik / Mazumder, Somnath / Das, Troyee / Pal, Uttam / Saha, Debanjan / De, Rudranil / Nag, Shiladitya / Banerjee, Chinmoy / Chandra Maiti, Nakul / Ghosh, Zhumur / Bandyopadhyay, Uday

    iScience

    2024  Volume 27, Issue 4, Page(s) 109384

    Abstract: Gastric cancer (GC) is a deadly malignancy that demands effective therapeutic intervention capitalizing unique drug target/s. Here, we report that indomethacin, a cyclooxygenase non-selective non-steroidal anti-inflammatory drug, arrests GC cell growth ... ...

    Abstract Gastric cancer (GC) is a deadly malignancy that demands effective therapeutic intervention capitalizing unique drug target/s. Here, we report that indomethacin, a cyclooxygenase non-selective non-steroidal anti-inflammatory drug, arrests GC cell growth by targeting mitochondrial deacetylase Sirtuin 3 (SIRT3). Interaction study revealed that indomethacin competitively inhibited SIRT3 by binding to nicotinamide adenine dinucleotide (NAD)-binding site. The Cancer Genome Atlas data meta-analysis indicated poor prognosis associated with high SIRT3 expression in GC. Further, transcriptome sequencing data of human gastric adenocarcinoma cells revealed that indomethacin treatment severely downregulated SIRT3. Indomethacin-induced SIRT3 downregulation augmented SOD2 and OGG1 acetylation, leading to mitochondrial redox dyshomeostasis, mtDNA damage, respiratory chain failure, bioenergetic crisis, mitochondrial fragmentation, and apoptosis via blocking the AMPK/PGC1α/SIRT3 axis. Indomethacin also downregulated SIRT3 regulators ERRα and PGC1α. Further, SIRT3 knockdown aggravated indomethacin-induced mitochondrial dysfunction as well as blocked cell-cycle progression to increase cell death. Thus, we reveal how indomethacin induces GC cell death by disrupting SIRT3 signaling.
    Language English
    Publishing date 2024-03-01
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2024.109384
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Metal ions provide structural stability and compactness to tetrameric purothionin

    Das, Swagata / Pal, Uttam / Chandra Maiti, Nakul

    RSC advances. 2016 Sept. 21, v. 6, no. 93

    2016  

    Abstract: Antimicrobial plant protein purothionin plays a significant role in immunity and microbial defense systems in plants and animals. From the molecular simulation analyses and spectroscopic investigation, it was observed that the structural arrangement of ... ...

    Abstract Antimicrobial plant protein purothionin plays a significant role in immunity and microbial defense systems in plants and animals. From the molecular simulation analyses and spectroscopic investigation, it was observed that the structural arrangement of the protein tetramer attained much more stable and compact conformation in the presence of calcium and magnesium compared to the tetramer alone in the absence of ions. An increase in the folded secondary structure in the presence of calcium and magnesium ions was observed. The circular dichroism spectral analysis and FT-IR study along with molecular dynamics simulation studies suggested some increase in the helical content/compactness of the protein. Structural stability of the protein, as observed, may be linked to increased antifungal activity against pathogens like Candida albicans, Candida krusei and Candida parapsilosis.
    Keywords Candida albicans ; Candida krusei ; Candida parapsilosis ; Fourier transform infrared spectroscopy ; antifungal properties ; calcium ; circular dichroism spectroscopy ; immunity ; magnesium ; metal ions ; molecular dynamics ; pathogens ; plant proteins ; spectral analysis
    Language English
    Dates of publication 2016-0921
    Size p. 90690-90700.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ISSN 2046-2069
    DOI 10.1039/c6ra16576a
    Database NAL-Catalogue (AGRICOLA)

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  3. Article: Identification of modes of interactions between 9-aminoacridine hydrochloride hydrate and serum proteins by low and high resolution spectroscopy and molecular modeling

    Mitra, Piyali / Pal, Uttam / Chandra Maiti, Nakul / Ghosh, Anirban / Bhunia, Anirban / Basu, Samita

    RSC advances. 2016 June 01, v. 6, no. 58

    2016  

    Abstract: Photophysical studies on binding interactions of a therapeutically important drug, 9-aminoacridine hydrochloride hydrate (9AA-HCl) with serum proteins, bovine serum albumin (BSA) and human serum albumin (HSA), have been performed using several low and ... ...

    Abstract Photophysical studies on binding interactions of a therapeutically important drug, 9-aminoacridine hydrochloride hydrate (9AA-HCl) with serum proteins, bovine serum albumin (BSA) and human serum albumin (HSA), have been performed using several low and high resolution spectroscopic techniques in conjunction with molecular modeling, which disclose some salient features of such interactions in ground and excited sates. The studies reveal that although 9AA-HCl forms ground state complexes with both BSA and HSA, their individual modes of binding interaction are quite different. Its resonance energy transfer efficiency is 79% and 72% with BSA and HSA respectively. It undergoes photoinduced electron transfer (PET) with BSA, but both PET and excited state proton transfer simultaneously with HSA, which are confirmed further by laser flash photolysis studies coupled with a magnetic field. Thermodynamic analyses indicate that the binding of 9AA-HCl with BSA and HSA is controlled primarily by changes in enthalpy and entropy, respectively, with corresponding binding stoichiometries of 1 : 1 and 1 : 2, respectively. Circular dichroism spectra depict some structural changes of both the serum proteins while interacting with 9AA-HCl. Docking analyses unveil the crucial role of the disparity between the cavity sizes of the proteins which might be the foremost reason behind the differential behavior of the drug towards BSA and HSA. The binding site pocket of HSA to be docked with 9AA-HCl is 1.7 times larger in dimensions than that of BSA, which facilitates HSA to bind with 9AA-HCl with higher stoichiometry compared to BSA. These differences in binding modes as well as affinities have been further confirmed by saturation transfer difference (STD) NMR experiments which show the ligand 9AA-HCl binds to BSA with higher affinity compared to HSA. In addition, unlike BSA, HSA can accommodate more than one ligand, which corroborates well with docking and fluorescence studies.
    Keywords binding sites ; bovine serum albumin ; circular dichroism spectroscopy ; drugs ; electron transfer ; energy transfer ; enthalpy ; entropy ; fluorescence ; human serum albumin ; ligands ; magnetic fields ; molecular models ; nuclear magnetic resonance spectroscopy ; photolysis ; stoichiometry
    Language English
    Dates of publication 2016-0601
    Size p. 53454-53468.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ISSN 2046-2069
    DOI 10.1039/c6ra04140j
    Database NAL-Catalogue (AGRICOLA)

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  4. Article: Binding of hemoglobin to ultrafine carbon nanoparticles: a spectroscopic insight into a major health hazard

    Banerji, Biswadip / Chandra Maiti, Nakul / Pal, Uttam / Pramanik, Sumit Kumar

    RSC advances. 2014 May 27, v. 4, no. 43

    2014  

    Abstract: Carbon nanoparticles (CNPs) are light and easily absorb into different parts of organs of the human body. They are suspended particulate matters of respirable sizes. In the atmosphere, ultrafine CNPs are known to be generated mainly from the combustion ... ...

    Abstract Carbon nanoparticles (CNPs) are light and easily absorb into different parts of organs of the human body. They are suspended particulate matters of respirable sizes. In the atmosphere, ultrafine CNPs are known to be generated mainly from the combustion of fuels and have been reported to be a major contributor to the induction of cardiopulmonary diseases. In third world countries, these diseases are more prevalent because of the higher abundance of ultrafine CNPs in the air. Different nanostructured materials, when exposed to the human body, can easily enter into the body through the lungs or other organs and tissues. In the laboratory, ultrafine carbon nanoparticles were synthesized and their structure was confirmed by DLS experiments, TEM and AFM imaging studies. Their interactions with hemoglobin (Hb) and myoglobin (Mb) were studied using fluorescence spectroscopy. The results indicate a remarkably strong interaction between carbon nanoparticles and Hb (or Mb). Temperature dependent steady state fluorescence spectroscopy showed exothermic binding of Hb to CNPs, which is favored by enthalpy and entropy changes. A circular dichroism study also indicated significant change in the protein secondary structure and a partial unfolding of the helical conformation. These findings are highly important for understanding the interactions between CNPs and Hb (or Mb), which might help to better clarify the potential risks and undesirable health hazards associated with carbon nanoparticles.
    Keywords atomic force microscopy ; carbon nanoparticles ; combustion ; developing countries ; enthalpy ; entropy ; fuels ; health hazards ; heat production ; hemoglobin ; image analysis ; lungs ; myoglobin ; particulates ; protein secondary structure ; risk ; temperature ; tissues
    Language English
    Dates of publication 2014-0527
    Size p. 22536-22541.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ISSN 2046-2069
    DOI 10.1039/c4ra02569e
    Database NAL-Catalogue (AGRICOLA)

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  5. Article: Stereoselective domino azidation and [3 + 2] cycloaddition: a facile route to chiral heterocyclic scaffolds from carbohydrate derived synthons

    Bhattacharya, Debleena / Chandra Maiti, Nakul / Chattopadhyay, Partha / Ghorai, Abhijit / Pal, Uttam

    RSC advances. 2013 Dec. 20, v. 4, no. 8

    2013  

    Abstract: A rapid one pot intermolecular aryl azidation and intramolecular azide-olefin cycloaddition protocol has been designed using carbohydrate precursors to generate optically active, aziridine fused oxa–aza heterocycles, related to DNA targeting anti-tumour ... ...

    Abstract A rapid one pot intermolecular aryl azidation and intramolecular azide-olefin cycloaddition protocol has been designed using carbohydrate precursors to generate optically active, aziridine fused oxa–aza heterocycles, related to DNA targeting anti-tumour agents which on further functionalization stereoselectively produce eight membered heterocyclic scaffolds. The structural conclusions were fully supported by a molecular modelling study based on density functional theory.
    Keywords antineoplastic agents ; aromatic compounds ; azides ; carbohydrates ; chemical derivatives ; chemical structure ; cycloaddition reactions ; density functional theory ; DNA ; ethyleneimine ; molecular models ; olefin ; stereoselective synthesis ; stereoselectivity
    Language English
    Dates of publication 2013-1220
    Size p. 4155-4162.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ISSN 2046-2069
    DOI 10.1039/c3ra45363d
    Database NAL-Catalogue (AGRICOLA)

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