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Interaction pattern for the complex of B-DNA Fullerene compounds with a set of known replication proteins using docking study
Fullerenes have attracted considerable attention due to their unique chemical structure and potential applications which has opened wide venues for possible human exposure to various fullerene types. Therefore, in depth knowledge of how fullerene may interfere with various cellular processes becomes...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Biomedical Informatics
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4421002/ https://www.ncbi.nlm.nih.gov/pubmed/25987764 http://dx.doi.org/10.6026/97320630011122 |
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author | Firdaus, Sumbul Dhasmana, Anupam Srivastava, Vandana Bano, Tasneem Fatima, Afreen Jamal, Qazi Mohammad Sajid Jahan, Roshan Wadhwad, Gulshan Lohani, Mohtashim |
author_facet | Firdaus, Sumbul Dhasmana, Anupam Srivastava, Vandana Bano, Tasneem Fatima, Afreen Jamal, Qazi Mohammad Sajid Jahan, Roshan Wadhwad, Gulshan Lohani, Mohtashim |
author_sort | Firdaus, Sumbul |
collection | PubMed |
description | Fullerenes have attracted considerable attention due to their unique chemical structure and potential applications which has opened wide venues for possible human exposure to various fullerene types. Therefore, in depth knowledge of how fullerene may interfere with various cellular processes becomes quite imperative. The present study was designed to investigate how the presence of fullerene affect the binding of DNA with different enzymes involved in replication process. Different fullerenes were first docked with DNA and then binding scores of different enzymes was analyzed with fullerene docked DNA. C30, C40 & C50 once docked with DNA, reduced the binding score of primase, whereas no significant change in the binding score was observed with the helicase, ssb protein, dna pol δ, dna pol ε, ligase, DNA clamp, and topoisomerases. On the contrast, the binding score of RPA14 decreases in fluctuating manner while interacting with increasing molecular weight of fullerene bound single-stranded DNA complex. The study revealed the affect of fullerene family interacting with DNA on the binding pattern of enzymes involved in replication process. Study suggests that the presence of most of fullerenes may not affect the activity of these enzymes necessary for replication process whereas C30, C40 & C50 may disrupt the activity of primase, (strating point for DNA polymerase) its docking score decreases from 13820 to 10702. |
format | Online Article Text |
id | pubmed-4421002 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
spelling | pubmed-44210022015-05-18 Interaction pattern for the complex of B-DNA Fullerene compounds with a set of known replication proteins using docking study Firdaus, Sumbul Dhasmana, Anupam Srivastava, Vandana Bano, Tasneem Fatima, Afreen Jamal, Qazi Mohammad Sajid Jahan, Roshan Wadhwad, Gulshan Lohani, Mohtashim Bioinformation Hypothesis Fullerenes have attracted considerable attention due to their unique chemical structure and potential applications which has opened wide venues for possible human exposure to various fullerene types. Therefore, in depth knowledge of how fullerene may interfere with various cellular processes becomes quite imperative. The present study was designed to investigate how the presence of fullerene affect the binding of DNA with different enzymes involved in replication process. Different fullerenes were first docked with DNA and then binding scores of different enzymes was analyzed with fullerene docked DNA. C30, C40 & C50 once docked with DNA, reduced the binding score of primase, whereas no significant change in the binding score was observed with the helicase, ssb protein, dna pol δ, dna pol ε, ligase, DNA clamp, and topoisomerases. On the contrast, the binding score of RPA14 decreases in fluctuating manner while interacting with increasing molecular weight of fullerene bound single-stranded DNA complex. The study revealed the affect of fullerene family interacting with DNA on the binding pattern of enzymes involved in replication process. Study suggests that the presence of most of fullerenes may not affect the activity of these enzymes necessary for replication process whereas C30, C40 & C50 may disrupt the activity of primase, (strating point for DNA polymerase) its docking score decreases from 13820 to 10702. Biomedical Informatics 2015-03-31 /pmc/articles/PMC4421002/ /pubmed/25987764 http://dx.doi.org/10.6026/97320630011122 Text en © 2015 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited. |
spellingShingle | Hypothesis Firdaus, Sumbul Dhasmana, Anupam Srivastava, Vandana Bano, Tasneem Fatima, Afreen Jamal, Qazi Mohammad Sajid Jahan, Roshan Wadhwad, Gulshan Lohani, Mohtashim Interaction pattern for the complex of B-DNA Fullerene compounds with a set of known replication proteins using docking study |
title | Interaction pattern for the complex of B-DNA Fullerene compounds with a set of known replication proteins using docking study |
title_full | Interaction pattern for the complex of B-DNA Fullerene compounds with a set of known replication proteins using docking study |
title_fullStr | Interaction pattern for the complex of B-DNA Fullerene compounds with a set of known replication proteins using docking study |
title_full_unstemmed | Interaction pattern for the complex of B-DNA Fullerene compounds with a set of known replication proteins using docking study |
title_short | Interaction pattern for the complex of B-DNA Fullerene compounds with a set of known replication proteins using docking study |
title_sort | interaction pattern for the complex of b-dna fullerene compounds with a set of known replication proteins using docking study |
topic | Hypothesis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4421002/ https://www.ncbi.nlm.nih.gov/pubmed/25987764 http://dx.doi.org/10.6026/97320630011122 |
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