Search for: structural-protein
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    Graphene-based nanoparticles as potential treatment options for parkinson’s disease: A molecular dynamics study

    , Article International Journal of Nanomedicine ; Volume 15 , 2020 , Pages 6887-6903 Alimohammadi, E ; Khedri, M ; Jahromi, A. M ; Maleki, R ; Rezaian, M ; Sharif University of Technology
    Dove Medical Press Ltd  2020
    Introduction: The study of abnormal aggregation of proteins in different tissues of the body has recently earned great attention from researchers in various fields of science. Concerning neurological diseases, for instance, the accumulation of amyloid fibrils can contribute to Parkinson’s disease, a progressively severe neurodegenerative disorder. The most prominent features of this disease are the degeneration of neurons in the substantia nigra and accumulation of α-synuclein aggregates, especially in the brainstem, spinal cord, and cortical areas. Dopamine replacement therapies and other medications have reduced motor impairment and had positive consequences on patients’ quality of life.... 

    Intracellular viral infection kinetics using a stochastic approach

    , Article Progress in Reaction Kinetics and Mechanism ; Volume 38, Issue 4 , 2013 , Pages 359-376 ; 14686783 (ISSN) Taherkhani, F ; Taherkhani, F ; Rezania, H ; Akbarzadeh, H ; Sharif University of Technology
    Stochastic simulation is carried out to investigate intracellular viral reaction kinetics and the time evolution of the average particle number ( N̄) and coefficient variation (CV) for genome, template, and structural protein. The coefficient variation of these components is found to be ordered as: CV template > CV structural protein > CVgenome. The average particle number is also calculated via a deterministic approach. The magnitude value of the difference between the stochastic and deterministic approaches is found to be N̄ template ̃ N̄ structural protein > N̄ genome. The Poisson algorithm has been used to investigate the number of particles in the dynamics of intracellular viral... 

    Failure tolerance of motif structure in biological networks

    , Article PLoS ONE ; Volume 6, Issue 5 , May , 2011 ; 19326203 (ISSN) Mirzasoleiman, B ; Jalili, M ; Sharif University of Technology
    Complex networks serve as generic models for many biological systems that have been shown to share a number of common structural properties such as power-law degree distribution and small-worldness. Real-world networks are composed of building blocks called motifs that are indeed specific subgraphs of (usually) small number of nodes. Network motifs are important in the functionality of complex networks, and the role of some motifs such as feed-forward loop in many biological networks has been heavily studied. On the other hand, many biological networks have shown some degrees of robustness in terms of their efficiency and connectedness against failures in their components. In this paper we... 

    Binding assessment of two arachidonic-based synthetic derivatives of adrenalin with β-lactoglobulin: Molecular modeling and chemometrics approach

    , Article Biophysical Chemistry ; Volume 207 , 2015 , Pages 97-106 ; 03014622 (ISSN) Gholami, S ; Bordbar, A. K ; Akvan, N ; Parastar, H ; Fani, N ; Gretskaya, N. M ; Bezuglov, V. V ; Haertlé, T ; Sharif University of Technology
    Elsevier  2015
    A computational approach to predict the main binding modes of two adrenalin derivatives, arachidonoyl adrenalin (AA-AD) and arachidonoyl noradrenalin (AA-NOR) with the β-lactoglubuline (BLG) as a nano-milk protein carrier is presented and assessed by comparison to the UV-Vis absorption spectroscopic data using chemometric analysis. Analysis of the spectral data matrices by using the multivariate curve resolution-alternating least squares (MCR-ALS) algorithm led to the pure concentration calculation and spectral profiles resolution of the chemical constituents and the apparent equilibrium constants computation. The negative values of entropy and enthalpy changes for both compound indicated... 

    Dual-sensitive hydrogel nanoparticles based on conjugated thermoresponsive copolymers and protein filaments for triggerable drug delivery

    , Article ACS Applied Materials and Interfaces ; Volume 10, Issue 23 , 17 May , 2018 , Pages 19336-19346 ; 19448244 (ISSN) Ghaffari, R ; Eslahi, N ; Tamjid, E ; Simchi, A ; Sharif University of Technology
    American Chemical Society  2018
    In this study, novel hydrogel nanoparticles with dual triggerable release properties based on fibrous structural proteins (keratin) and thermoresponsive copolymers (Pluronic) are introduced. Nanoparticles were used for curcumin delivery as effective and safe anticancer agents, the hydrophobicity of which has limited their clinical applications. A drug was loaded into hydrogel nanoparticles by a single-step nanoprecipitation method. The drug-loaded nanoparticles had an average diameter of 165 and 66 nm at 25 and 37 °C, respectively. It was shown that the drug loading efficiency could be enhanced through crosslinking of the disulfide bonds in keratin. Crosslinking provided a targeted release... 

    Identification of a novel multifunctional ligand for simultaneous inhibition of amyloid-beta (aβ42) and chelation of zinc metal ion

    , Article ACS Chemical Neuroscience ; Volume 10, Issue 11 , 2019 , Pages 4619-4632 ; 19487193 (ISSN) Asadbegi, M ; Shamloo, A ; Sharif University of Technology
    American Chemical Society  2019
    Zinc binding to β-amyloid structure could promote amyloid-β aggregation, as well as reactive oxygen species (ROS) production, as suggested in many experimental and theoretical studies. Therefore, the introduction of multifunctional drugs capable of chelating zinc metal ion and inhibiting Aβ aggregation is a promising strategy in the development of AD treatment. The present study has evaluated the efficacy of a new bifunctional peptide drug using molecular docking and molecular dynamics (MD) simulations. This drug comprises two different domains, an inhibitor domain, obtained from the C-terminal hydrophobic region of Aβ, and a Zn2+ chelating domain, derived from rapeseed meal, merge with a... 

    Structural stability and sustained release of protein from a multilayer nanofiber/nanoparticle composite

    , Article International Journal of Biological Macromolecules ; Volume 75 , April , 2015 , Pages 248-257 ; 01418130 (ISSN) Vakilian, S ; Mashayekhan, S ; Shabani, I ; Khorashadizadeh, M ; Fallah, A ; Soleimani, M ; Sharif University of Technology
    Elsevier  2015
    The cellular microenvironment can be engineered through the utilization of various nano-patterns and matrix-loaded bioactive molecules. In this study, a multilayer system of electrospun scaffold containing chitosan nanoparticles was introduced to overcome the common problems of instability and burst release of proteins from nanofibrous scaffolds. Bovine serum albumin (BSA)-loaded chitosan nanoparticles was fabricated based on ionic gelation interaction between chitosan and sodium tripolyphosphate. Suspension electrospinning was employed to fabricate poly-e{open}-caprolacton (PCL) containing protein-loaded chitosan nanoparticles with a core-shell structure. To obtain the desired scaffold... 

    Interaction of copper(II) complex of compartmental Schiff base ligand N,N′-bis(3-hydroxysalicylidene)ethylenediamine with bovine serum albumin

    , Article Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy ; Volume 66, Issue 3 , 2007 , Pages 650-655 ; 13861425 (ISSN) Boghaei, D. M ; Farvid, S. S ; Gharagozlou, M ; Sharif University of Technology
    Circular dichroism (CD) spectroscopy, cyclic voltammetry (CV) and differential pulse voltammetry (DPV) were used to investigate the interaction between copper(II) complex of compartmental Schiff base ligand (L), N,N′-bis(3-hydroxysalicylidene)ethylenediamine, and bovine serum albumin (BSA) in 0.1 mol dm-3 phosphate buffer solution adjusted to physiological pH 7.0 containing 20% (w/w) dimethylsulfoxide at room temperature. CD spectra show that the interaction of the copper(II) complex with BSA leads to changes in the α-helical content of BSA and therefore changes in secondary structure of the protein with the slight red shift (2 nm) in CD spectra. From the voltammetric data, i.e. changes in...