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A Colorimetric Assay of Dna Methyltransferase Activity Based on Peroxidase Mimicking of Dna Template Ag/Pt Bimetallic Nanoclusters Publisher Pubmed



Kermani HA1 ; Hosseini M1 ; Miti A2 ; Dadmehr M3 ; Zuccheri G2 ; Hosseinkhani S4 ; Ganjali MR5, 6
Authors
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Authors Affiliations
  1. 1. Department of Life Science Engineering, Faculty of New Sciences and Technologies, University of Tehran, Amir Abad, North Kargar St, Tehran, 1417466191, Iran
  2. 2. Department of Pharmacy and Biotechnology and Interdepartmental Center for Industrial Research on Health Sciences and Technologies at the University of Bologna, The Nanoscience Institute of CNR, the National Interuniversity Consortium of Materials Science and Technology, Via Irnerio, 48, Bologna, 40126, Italy
  3. 3. Department of Biotechnology, Payame Noor University, Lashkarak Rd, P.O. Box 19395-4697, Tehran, Iran
  4. 4. Department of Biochemistry, Tarbiat Modares University, Jalal AleAhmad Nasr, P.O. Box 14115-111, Tehran, Iran
  5. 5. Center of Excellence in Electrochemistry, School of Chemistry, College of Science, University of Tehran, 16th Azar St., Enghelab Sq, P.O. Box 14155-6619, Tehran, Iran
  6. 6. Biosensor Research Center, Endocrinology and Metabolism Molecular-Cellular Sciences Institute, Tehran University of Medical Sciences, No 10 Jalale Al Ahmad St, Tehran, 1411713137, Iran

Source: Analytical and Bioanalytical Chemistry Published:2018


Abstract

DNA methylation catalyzed by DNA methyl transferase (MTase) is a significant epigenetic process for modulating gene expression. Abnormal levels of DNA MTase enzyme have been regarded as a cancer biomarker or a sign of bacterial diseases. We developed a novel colorimetric method to assay M.SssI MTase activity employing peroxidase-like activity of DNA template Ag/Pt NCs without using restriction enzymes. Based on inhibiting the peroxidase reaction that occurred in the TMB-H2O2 system, in the presence of MTase, a highly sensitive and selective colorimetric biosensor was fabricated with a detection limit (LOD) of 0.05 U/mL and a linear range from 0.5 to 10 U/mL. The changes in absorption intensity were monitored to quantify the M.SssI activity. This strategy had a high selectivity over other proteins. Furthermore, it is also demonstrated that this method can be used for the evaluation and screening of inhibitors for DNA MTase. © 2018, Springer-Verlag GmbH Germany, part of Springer Nature.
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