In silico studies of the interaction of the colon cancer receptor and RNA aptamer adsorbed on (1 0 1) facet of TiO 2 nan
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In silico studies of the interaction of the colon cancer receptor and RNA aptamer adsorbed on (1 0 1) facet of TiO2 nanoparticle investigated by molecular dynamics simulation Mohaddeseh Habibzadeh Mashatooki1,2,3 · Amirali Abbasi1,2,3 · Jaber Jahanbin Sardroodi1,2,3 Received: 27 January 2019 / Revised: 18 May 2019 / Accepted: 29 May 2019 © Springer Science+Business Media, LLC, part of Springer Nature 2019
Abstract The epidermal growth factor receptor (EGFR) is a trans-membrane protein which belongs to the ErbB family of receptor tyrosine kinases (RTK). The peptide growth factors of the EGF-family of proteins activated these trans-membrane proteins by binding to them. In order to blocking these receptors and prevent over-expression in human carcinomas, we used a potential anticancer RNA aptamer. The RNA aptamer was delivered to the target receptor with the TiO2 nanosheet using the molecular dynamics simulation. The structural and energetic parameters were measure and analyzed in detail. The root mean square deviation and fluctuation and center of mass of components were calculated. Besides, the hydrogen bonds were considered to investigate the effect of water molecules. The van de Waals and electrostatics contributions depict the attractive force between RNA aptamer and the receptor. Our results suggest that for better interaction of RNA aptamer and receptor, first the RNA aptamer should release from the Nano carrier surface.
Keywords Molecular dynamics · Biocompatible nanosheet · Growth factor receptor · RNA aptamer · Binding mechanism · Cancer therapy
1 Introduction * Mohaddeseh Habibzadeh Mashatooki [email protected] * Jaber Jahanbin Sardroodi [email protected] Extended author information available on the last page of the article
Cell surface receptors and growth factor interactions influence survival and metabolism in the human body [1, 2]. Intracellular portion of the receptor, changes as the growth
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factor binds to the membrane receptor. The earliest characterized members of the growth factor/receptor tyrosine kinase (RTK) family are the epidermal growth factor receptor (EGFR,1 also ErbB1 or HER1) and its ligands, epidermal growth factor (EGF) and transforming growth factor [1]. Among the different families of growth factors and growth factor receptors, the epidermal growth factor receptor (EGFR) and the EGF-family of peptide growth factor have a major role in the progression and over-expression of different carcinoma types [3–5]. In the early embryonic development and in the renewal of stem cells in normal tissues such as the skin, the EGF ligand/receptor system is also contributed [6, 7] The role of EGFR in the pathogenesis of human carcinoma has been mentioned in several review articles. The ligands bind to the extracellular domain of receptors, which form the receptor homo- or heterodimers, and activate the intrinsic tyrosine kinase domain subsequently [8–10]. The extracellular domain of each ErbB receptor consists of four subdomains (I–IV). Subd
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