Molecular Docking Evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one Derivatives as Selective Bacterial Adenylate Kinase Inhibitors

Molecular Docking Evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one Derivatives as Selective Bacterial Adenylate Kinase Inhibitors

Multi-drug resistant microorganism infections with emerging problems that require not only a prevention strategy, but also the development of new inhibitory compounds. Six previously synthesized 5-arylidene-2-thioxothiazolidin-4-one derivatives 1a–f, were screened for inhibitory activity o...

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Main Authors: Mihaela Ileana Ionescu, Ovidiu Oniga
Format: Article
Language:English
Published: MDPI AG 2018-05-01
Series:Molecules
Subjects:
adenylate kinase
thiazolidine
molecular docking
inhibitory activity
Online Access:http://www.mdpi.com/1420-3049/23/5/1076
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spelling doaj-e0db9354822a42e6b82e476387ad9dc72020-11-24T23:53:20ZengMDPI AGMolecules1420-30492018-05-01235107610.3390/molecules23051076molecules23051076Molecular Docking Evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one Derivatives as Selective Bacterial Adenylate Kinase InhibitorsMihaela Ileana Ionescu0Ovidiu Oniga1Department of Microbiology, Iuliu Hațieganu University of Medicine and Pharmacy, 400349 Cluj-Napoca, RomaniaDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, Iuliu Hațieganu University of Medicine and Pharmacy, 400012 Cluj-Napoca, RomaniaMulti-drug resistant microorganism infections with emerging problems that require not only a prevention strategy, but also the development of new inhibitory compounds. Six previously synthesized 5-arylidene-2-thioxothiazolidin-4-one derivatives 1a–f, were screened for inhibitory activity on adenylate kinases of different origins by molecular docking. The compounds 1c and 1d were the most efficient inhibitors of bacterial and some archean adenylate kinases. Hydrogen bond interactions were observed with the residues belonging to the ATP binding site. Moreover human adenylate kinases are poor targets, suggesting that this selectivity offers promising prospectives for refining the structure of our compounds.http://www.mdpi.com/1420-3049/23/5/1076adenylate kinasethiazolidinemolecular dockinginhibitory activity
collection DOAJ
language English
format Article
sources DOAJ
author Mihaela Ileana Ionescu
Ovidiu Oniga
spellingShingle Mihaela Ileana Ionescu
Ovidiu Oniga
Molecular Docking Evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one Derivatives as Selective Bacterial Adenylate Kinase Inhibitors
Molecules
adenylate kinase
thiazolidine
molecular docking
inhibitory activity
author_facet Mihaela Ileana Ionescu
Ovidiu Oniga
author_sort Mihaela Ileana Ionescu
title Molecular Docking Evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one Derivatives as Selective Bacterial Adenylate Kinase Inhibitors
title_short Molecular Docking Evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one Derivatives as Selective Bacterial Adenylate Kinase Inhibitors
title_full Molecular Docking Evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one Derivatives as Selective Bacterial Adenylate Kinase Inhibitors
title_fullStr Molecular Docking Evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one Derivatives as Selective Bacterial Adenylate Kinase Inhibitors
title_full_unstemmed Molecular Docking Evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one Derivatives as Selective Bacterial Adenylate Kinase Inhibitors
title_sort molecular docking evaluation of (e)-5-arylidene-2-thioxothiazolidin-4-one derivatives as selective bacterial adenylate kinase inhibitors
publisher MDPI AG
series Molecules
issn 1420-3049
publishDate 2018-05-01
description Multi-drug resistant microorganism infections with emerging problems that require not only a prevention strategy, but also the development of new inhibitory compounds. Six previously synthesized 5-arylidene-2-thioxothiazolidin-4-one derivatives 1a–f, were screened for inhibitory activity on adenylate kinases of different origins by molecular docking. The compounds 1c and 1d were the most efficient inhibitors of bacterial and some archean adenylate kinases. Hydrogen bond interactions were observed with the residues belonging to the ATP binding site. Moreover human adenylate kinases are poor targets, suggesting that this selectivity offers promising prospectives for refining the structure of our compounds.
topic adenylate kinase
thiazolidine
molecular docking
inhibitory activity
url http://www.mdpi.com/1420-3049/23/5/1076
work_keys_str_mv AT mihaelaileanaionescu moleculardockingevaluationofe5arylidene2thioxothiazolidin4onederivativesasselectivebacterialadenylatekinaseinhibitors
AT ovidiuoniga moleculardockingevaluationofe5arylidene2thioxothiazolidin4onederivativesasselectivebacterialadenylatekinaseinhibitors
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