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    Physiological temperature has a crucial role in amyloid beta in the absence and presence of hydrophobic and hydrophilic nanoparticles

    , Article ACS Chemical Neuroscience ; Volume 4, Issue 3 , December , 2013 , Pages 375-378 ; 19487193 (ISSN) Ghavami, M ; Rezaei, M ; Ejtehadi, R ; Lotfi, M ; Shokrgozar, M. A ; Abd Emamy, B ; Raush, J ; Mahmoudi, M ; Sharif University of Technology
    2013
    Abstract
    Amyloid beta fibrillation can lead to major disorder of neurons processes and is associated with several neuronal diseases (e.g., Alzheimer's disease). We report here an importance of slight temperature changes, in the physiological range (35-42 °C), on the amyloid fibrillation process in the presence and absence of hydrophilic (silica) and hydrophobic (polystyrene) nanoparticles (NPs). The results highlight the fact that slight increases in temperature can induce inhibitory and acceleratory effects of hydrophobic and hydrophilic NPs on the fibrillation process, respectively. Using further in vivo considerations, the outcomes of this study can be used for considerable modifications on the... 

    Effects of temperature shifts and oscillations on recombinant protein production expressed in Escherichia coli

    , Article Bioprocess and Biosystems Engineering ; Volume 36, Issue 11 , 2013 , Pages 1571-1577 ; 16157591 (ISSN) Jazini, M ; Herwig, C ; Sharif University of Technology
    2013
    Abstract
    Escherichia coli is widely used host for the intracellular expression of many proteins. However, in some cases also secretion of protein from periplasm was observed. Improvement of both intracellular and extracellular production of recombinant protein in E. coli is an attractive goal in order to reduce production cost and increase process efficiency and economics. Since heat shock proteins in E. coli were reported to be helpful for protein refolding and hindering aggregation, in this work different types of single and periodic heat shocks were tested on lab scale to enhance intracellular and extracellular protein production. A single heat shock prior to induction and different oscillatory... 

    Heat transfer of PEGylated cobalt ferrite nanofluids for magnetic fluid hyperthermia therapy: In vitro cellular study

    , Article Journal of Magnetism and Magnetic Materials ; Volume 462 , 2018 , Pages 185-194 ; 03048853 (ISSN) Hatamie, S ; Parseh, B ; Ahadian, M. M ; Naghdabadi, F ; Saber, R ; Soleimani, M ; Sharif University of Technology
    Elsevier B.V  2018
    Abstract
    Hyperthermia generally means as increasing the temperature of particular region of body to rise 5 °C above the body's physiological temperature. Here, we investigate the thermal therapy of PEGylated cobalt ferrite nanoparticles prepared by hydrothermal approach on cancerous cell line in the alternative current magnetic field. To characterize of the magnetic nanoparticles (MNPs), scanning electron microscopy, dynamic light scattering, X-ray diffraction, Fourier transform infrared spectroscopy, and vibrating sample magnetometer were used. X-ray diffraction analysis confirmed the spinel phase formation of the MNPs. Cytotoxicity of MNPs using MTT assay on L929 cell lines showed the PEGylated... 

    Examination of chondroitinase ABC I immobilization onto dextran-coated Fe3O4 nanoparticles and its in-vitro release

    , Article Journal of Biotechnology ; Volume 309 , 2020 , Pages 131-141 Askaripour, H ; Vossoughi, M ; Khajeh, K ; Alemzadeh, I ; Sharif University of Technology
    Elsevier B.V  2020
    Abstract
    Chondroitinase ABC I (cABC I) has received notable attention in treatment of spinal cord injuries and its application as therapeutics has been limited due to low thermal stability at physiological temperature. In this study, cABC I enzyme was immobilized on the dextran-coated Fe3O4 nanoparticles through physical adsorption to improve the thermal stability. The nanoparticles were characterized using XRD, SEM, VSM, and FTIR analyses. Response surface methodology and central composite design were employed to assess factors affecting the activity of immobilized cABC I. Experimental results showed that pH 6.3, temperature 24 °C, enzyme/support mass ratio 1.27, and incubation time 5.7 h were the...