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  1. Article ; Online: Correction to “Porphyrin–Gold Nanomaterial for Efficient Drug Delivery to Cancerous Cells”

    Kaushik Bera / Samarpan Maiti / Mritunjoy Maity / Chitra Mandal / Nakul C. Maiti

    ACS Omega, Vol 7, Iss 2, Pp 2484-

    2022  Volume 2485

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2022-01-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Dabrafenib, idelalisib and nintedanib act as significant allosteric modulator for dengue NS3 protease.

    R V Sriram Uday / Rajdip Misra / Annaram Harika / Sandip Dolui / Achintya Saha / Uttam Pal / V Ravichandiran / Nakul C Maiti

    PLoS ONE, Vol 16, Iss 9, p e

    2021  Volume 0257206

    Abstract: Dengue virus (DENV) encodes a unique protease (NS3/NS2B) essential for its maturation and infectivity and, it has become a key target for anti-viral drug design to treat dengue and other flavivirus related infections. Present investigation established ... ...

    Abstract Dengue virus (DENV) encodes a unique protease (NS3/NS2B) essential for its maturation and infectivity and, it has become a key target for anti-viral drug design to treat dengue and other flavivirus related infections. Present investigation established that some of the drug molecules currently used mainly in cancer treatment are susceptible to bind non-active site (allosteric site/ cavity) of the NS3 protease enzyme of dengue virus. Computational screening and molecular docking analysis found that dabrafenib, idelalisib and nintedanib can bind at the allosteric site of the enzyme. The binding of the molecules to the allosteric site found to be stabilized via pi-cation and hydrophobic interactions, hydrogen-bond formation and π-stacking interaction with the molecules. Several interacting residues of the enzyme were common in all the five serotypes. However, the interaction/stabilizing forces were not uniformly distributed; the π-stacking was dominated with DENV3 proteases, whereas, a charged/ionic interaction was the major force behind interaction with DENV2 type proteases. In the allosteric cavity of protease from DENV1, the residues Lys73, Lys74, Thr118, Glu120, Val123, Asn152 and Ala164 were involved in active interaction with the three molecules (dabrafenib, idelalisib and nintedanib). Molecular dynamics (MD) analysis further revealed that the molecules on binding to NS3 protease caused significant changes in structural fluctuation and gained enhanced stability. Most importantly, the binding of the molecules effectively perturbed the protein conformation. These changes in the protein conformation and dynamics could generate allosteric modulation and thus may attenuate/alter the NS3 protease functionality and mobility at the active site. Experimental studies may strengthen the notion whether the binding reduce/enhance the catalytic activity of the enzyme, however, it is beyond the scope of this study.
    Keywords Medicine ; R ; Science ; Q
    Subject code 540
    Language English
    Publishing date 2021-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Envisaging the Structural Elevation in the Early Event of Oligomerization of Disordered Amyloid β Peptide

    Anupam Roy / Kousik Chandra / Sandip Dolui / Nakul C. Maiti

    ACS Omega, Vol 2, Iss 8, Pp 4316-

    2017  Volume 4327

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2017-08-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Structural Insight of Amyloidogenic Intermediates of Human Insulin

    Sandip Dolui / Anupam Roy / Uttam Pal / Achintya Saha / Nakul C. Maiti

    ACS Omega, Vol 3, Iss 2, Pp 2452-

    2018  Volume 2462

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2018-02-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Porphyrin–Gold Nanomaterial for Efficient Drug Delivery to Cancerous Cells

    Kaushik Bera / Samarpan Maiti / Mritunjoy Maity / Chitra Mandal / Nakul C. Maiti

    ACS Omega, Vol 3, Iss 4, Pp 4602-

    2018  Volume 4619

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2018-04-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Orientation of tyrosine side chain in neurotoxic Aβ differs in two different secondary structures of the peptide

    Swagata Das / Supriya Das / Anupam Roy / Uttam Pal / Nakul C. Maiti

    Royal Society Open Science, Vol 3, Iss

    2016  Volume 10

    Abstract: Amyloid β (Aβ) peptide is present as a major component in amyloid plaque that is one of the hallmarks of Alzheimer's disease. The peptide contains a single tyrosine residue and Aβ has a major implication in the pathology of the disease progression. ... ...

    Abstract Amyloid β (Aβ) peptide is present as a major component in amyloid plaque that is one of the hallmarks of Alzheimer's disease. The peptide contains a single tyrosine residue and Aβ has a major implication in the pathology of the disease progression. Current investigation revealed that the tyrosine side chain attained two different critical stereo orientations in two dissimilar conformational states of the peptide. The extended α-helical structure of the peptide observed in an apolar solvent or methanol/water mixture became disordered in aqueous medium and the radius of gyration decreased. In aqueous medium, the torsional angle around Cα–Cβ of tyrosine group became −60°. However, in its α-helical conformation in an apolar system, the measured angle was 180° and this rotameric state may be reasoned behind stronger tyrosine fluorescence compared with the disordered state of the peptide. Molecular dynamics simulation analyses and spectroscopic studies have helped us to understand the major structural changes in the secondary structure of the peptide in the two conformational states. A conformational clustering indicated that the compact state is more stable with tyrosine residue attaining the torsion angle value of −60°, whereas the native state (in HFIP/water mixture) is prevalent at a torsion angle value of −180°. High solvent accessibility has possibly stabilized the particular rotameric state (−60°) of the tyrosine residue and could be the reason behind decrease in fluorescence of the sole tyrosine residue in an aqueous buffer solution (pH 7.4) compared with its fluorescence in the α-helical structure in the micellar environment.
    Keywords aβ peptide ; tyrosine fluorescence ; conformation ; rotamer ; Science ; Q
    Subject code 540
    Language English
    Publishing date 2016-01-01T00:00:00Z
    Publisher The Royal Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.

    Swagata Das / Uttam Pal / Supriya Das / Khyati Bagga / Anupam Roy / Arpita Mrigwani / Nakul C Maiti

    PLoS ONE, Vol 9, Iss 3, p e

    2014  Volume 89781

    Abstract: An amyloidogenic region (AR) in a protein sequence plays a significant role in protein aggregation and amyloid formation. We have investigated the sequence complexity of AR that is present in intrinsically disordered human proteins. More than 80% human ... ...

    Abstract An amyloidogenic region (AR) in a protein sequence plays a significant role in protein aggregation and amyloid formation. We have investigated the sequence complexity of AR that is present in intrinsically disordered human proteins. More than 80% human proteins in the disordered protein databases (DisProt+IDEAL) contained one or more ARs. With decrease of protein disorder, AR content in the protein sequence was decreased. A probability density distribution analysis and discrete analysis of AR sequences showed that ∼8% residue in a protein sequence was in AR and the region was in average 8 residues long. The residues in the AR were high in sequence complexity and it seldom overlapped with low complexity regions (LCR), which was largely abundant in disorder proteins. The sequences in the AR showed mixed conformational adaptability towards α-helix, β-sheet/strand and coil conformations.
    Keywords Medicine ; R ; Science ; Q
    Subject code 612
    Language English
    Publishing date 2014-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: 2,2'-diphenyl-3,3'-diindolylmethane

    Arijit Bhowmik / Nilanjana Das / Uttam Pal / Madhumita Mandal / Seemana Bhattacharya / Moumita Sarkar / Parasuraman Jaisankar / Nakul C Maiti / Mrinal K Ghosh

    PLoS ONE, Vol 8, Iss 3, p e

    a potent compound induces apoptosis in breast cancer cells by inhibiting EGFR pathway.

    2013  Volume 59798

    Abstract: Despite recent advances in medicine, 30-40% of patients with breast cancer show recurrence underscoring the need for improved effective therapy. In this study, by in vitro screening we have selected a novel synthetic indole derivative 2,2'-diphenyl-3,3'- ... ...

    Abstract Despite recent advances in medicine, 30-40% of patients with breast cancer show recurrence underscoring the need for improved effective therapy. In this study, by in vitro screening we have selected a novel synthetic indole derivative 2,2'-diphenyl-3,3'-diindolylmethane (DPDIM) as a potential anti- breast cancer agent. DPDIM induces apoptosis both in vitro in breast cancer cells MCF7, MDA-MB 231 and MDA-MB 468 and in vivo in 7,12-dimethylbenz[α]anthracene (DMBA) induced Sprague-Dawley (SD) rat mammary tumor. Our in vitro studies show that DPDIM exerts apoptotic effect by negatively regulating the activity of EGFR and its downstream molecules like STAT3, AKT and ERK1/2 which are involved in the proliferation and survival of these cancer cells. In silico predictions also suggest that DPDIM may bind to EGFR at its ATP binding site. DPDIM furthermore inhibits EGF induced increased cell viability. We have also shown decreased expression of pro-survival factor Bcl-XL as well as increase in the level of pro-apoptotic proteins like Bax, Bad, Bim in DPDIM treated cells in vitro and in vivo. Our results further indicate that the DPDIM induced apoptosis is mediated through mitochondrial apoptotic pathway involving the caspase-cascade. To the best of our knowledge this is the first report of DPDIM for its anticancer activity. Altogether this report suggests that DPDIM could be an effective therapeutic agent for breast cancer.
    Keywords Medicine ; R ; Science ; Q
    Subject code 616 ; 610
    Language English
    Publishing date 2013-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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