Design and examine oligonucleotide structures as inhibitors to topoisomerase IV

Topoisomerase IV is an enzyme that exclusively presents in prokaryotic cells and is mainly responsible for unwinding interlocked DNA strands at the final stage of prokaryotic replication. Since it is a prokaryotic enzyme, various types of quinolones were developed in the past as inhibitors of topo I...

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Main Author: Guo, Juanjuan
Other Authors: Shao Fangwei
Format: Theses and Dissertations
Language:English
Published: 2014
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Online Access:http://hdl.handle.net/10356/61861
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-618612023-02-28T23:41:51Z Design and examine oligonucleotide structures as inhibitors to topoisomerase IV Guo, Juanjuan Shao Fangwei School of Physical and Mathematical Sciences DRNTU::Science Topoisomerase IV is an enzyme that exclusively presents in prokaryotic cells and is mainly responsible for unwinding interlocked DNA strands at the final stage of prokaryotic replication. Since it is a prokaryotic enzyme, various types of quinolones were developed in the past as inhibitors of topo IV for treating bacterial infection. In consideration that bacterial resistance to antibiotics has occurred constantly, new types of oligonucleotides as topo IV inhibitors have been examined during our recent investigations, which include those that contain nick sites, gap, mismatched and overhang structures. Among them, the nick-, gap- and mismatched base pair-containing oligonucleotides displayed significantly high inhibitory effects toward topo IV. It is our anticipation that the outcomes of our investigation could be beneficial for pharmaceutical companies for evaluating the possibility of topo IV oligonucleotide inhibitors as antibiotics once tools for transfection of oligonucleotides into bacteria will be validated in the future. ​Master of Science 2014-12-03T05:16:03Z 2014-12-03T05:16:03Z 2014 2014 Thesis http://hdl.handle.net/10356/61861 en 50 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science
spellingShingle DRNTU::Science
Guo, Juanjuan
Design and examine oligonucleotide structures as inhibitors to topoisomerase IV
description Topoisomerase IV is an enzyme that exclusively presents in prokaryotic cells and is mainly responsible for unwinding interlocked DNA strands at the final stage of prokaryotic replication. Since it is a prokaryotic enzyme, various types of quinolones were developed in the past as inhibitors of topo IV for treating bacterial infection. In consideration that bacterial resistance to antibiotics has occurred constantly, new types of oligonucleotides as topo IV inhibitors have been examined during our recent investigations, which include those that contain nick sites, gap, mismatched and overhang structures. Among them, the nick-, gap- and mismatched base pair-containing oligonucleotides displayed significantly high inhibitory effects toward topo IV. It is our anticipation that the outcomes of our investigation could be beneficial for pharmaceutical companies for evaluating the possibility of topo IV oligonucleotide inhibitors as antibiotics once tools for transfection of oligonucleotides into bacteria will be validated in the future.
author2 Shao Fangwei
author_facet Shao Fangwei
Guo, Juanjuan
format Theses and Dissertations
author Guo, Juanjuan
author_sort Guo, Juanjuan
title Design and examine oligonucleotide structures as inhibitors to topoisomerase IV
title_short Design and examine oligonucleotide structures as inhibitors to topoisomerase IV
title_full Design and examine oligonucleotide structures as inhibitors to topoisomerase IV
title_fullStr Design and examine oligonucleotide structures as inhibitors to topoisomerase IV
title_full_unstemmed Design and examine oligonucleotide structures as inhibitors to topoisomerase IV
title_sort design and examine oligonucleotide structures as inhibitors to topoisomerase iv
publishDate 2014
url http://hdl.handle.net/10356/61861
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