Molecular Docking Study of Phthalimide Derivatives as Non-nucleoside HIV-1 Reverse Transcriptase Inhibitor

Molecular Docking Study of Phthalimide Derivatives as Non-nucleoside HIV-1 Reverse Transcriptase Inhibitor

The molecular docking approach was used to determine the binding affinities and the interactions of Mycobacterium tuberculosis dihydrofolate reductase (mtbDHFR) in complex with 2, 4-diaminopyrimidines analogues (PYR analogous). This approach can classify compounds into low and high affinity agents w...

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Main Authors: Pimonluck Sittikornpaiboon, Pisanu Toochinda, Chawanee Thongpanchang, Ubolsree Leartsakulpanich, Luckhana Lawtrakul
Format: บทความวารสาร
Language:English
Published: Science Faculty of Chiang Mai University 2019
Online Access:http://it.science.cmu.ac.th/ejournal/dl.php?journal_id=7351
http://cmuir.cmu.ac.th/jspui/handle/6653943832/63791
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Institution: Chiang Mai University
Language: English
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spelling th-cmuir.6653943832-637912019-05-07T09:57:18Z Molecular Docking Study of Phthalimide Derivatives as Non-nucleoside HIV-1 Reverse Transcriptase Inhibitor Pimonluck Sittikornpaiboon Pisanu Toochinda Chawanee Thongpanchang Ubolsree Leartsakulpanich Luckhana Lawtrakul The molecular docking approach was used to determine the binding affinities and the interactions of Mycobacterium tuberculosis dihydrofolate reductase (mtbDHFR) in complex with 2, 4-diaminopyrimidines analogues (PYR analogous). This approach can classify compounds into low and high affinity agents which can be further developed as a possible dihydrofolate reductase inhibitor for tuberculosis treatment. Our study provides insight into the important interactions of mtbDHFR with PYR analogues which lead to the design of effective agents against mtbDHFR. 2019-05-07T09:57:18Z 2019-05-07T09:57:18Z 2016 บทความวารสาร 0125-2526 http://it.science.cmu.ac.th/ejournal/dl.php?journal_id=7351 http://cmuir.cmu.ac.th/jspui/handle/6653943832/63791 Eng Science Faculty of Chiang Mai University
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
language English
description The molecular docking approach was used to determine the binding affinities and the interactions of Mycobacterium tuberculosis dihydrofolate reductase (mtbDHFR) in complex with 2, 4-diaminopyrimidines analogues (PYR analogous). This approach can classify compounds into low and high affinity agents which can be further developed as a possible dihydrofolate reductase inhibitor for tuberculosis treatment. Our study provides insight into the important interactions of mtbDHFR with PYR analogues which lead to the design of effective agents against mtbDHFR.
format บทความวารสาร
author Pimonluck Sittikornpaiboon
Pisanu Toochinda
Chawanee Thongpanchang
Ubolsree Leartsakulpanich
Luckhana Lawtrakul
spellingShingle Pimonluck Sittikornpaiboon
Pisanu Toochinda
Chawanee Thongpanchang
Ubolsree Leartsakulpanich
Luckhana Lawtrakul
Molecular Docking Study of Phthalimide Derivatives as Non-nucleoside HIV-1 Reverse Transcriptase Inhibitor
author_facet Pimonluck Sittikornpaiboon
Pisanu Toochinda
Chawanee Thongpanchang
Ubolsree Leartsakulpanich
Luckhana Lawtrakul
author_sort Pimonluck Sittikornpaiboon
title Molecular Docking Study of Phthalimide Derivatives as Non-nucleoside HIV-1 Reverse Transcriptase Inhibitor
title_short Molecular Docking Study of Phthalimide Derivatives as Non-nucleoside HIV-1 Reverse Transcriptase Inhibitor
title_full Molecular Docking Study of Phthalimide Derivatives as Non-nucleoside HIV-1 Reverse Transcriptase Inhibitor
title_fullStr Molecular Docking Study of Phthalimide Derivatives as Non-nucleoside HIV-1 Reverse Transcriptase Inhibitor
title_full_unstemmed Molecular Docking Study of Phthalimide Derivatives as Non-nucleoside HIV-1 Reverse Transcriptase Inhibitor
title_sort molecular docking study of phthalimide derivatives as non-nucleoside hiv-1 reverse transcriptase inhibitor
publisher Science Faculty of Chiang Mai University
publishDate 2019
url http://it.science.cmu.ac.th/ejournal/dl.php?journal_id=7351
http://cmuir.cmu.ac.th/jspui/handle/6653943832/63791
_version_ 1681425960959737856

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