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Synthesis, Antimicrobial Activity and Molecular Docking Studies of 1,3‐Thiazole Derivatives Incorporating Adamantanyl Moiety
Author(s) -
Łączkowski K. Z.,
Misiura K.,
Biernasiuk A.,
Malm A.,
Paneth A.,
Plech T.
Publication year - 2016
Publication title -
journal of heterocyclic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.321
H-Index - 59
eISSN - 1943-5193
pISSN - 0022-152X
DOI - 10.1002/jhet.2364
Subject(s) - chemistry , bacillus subtilis , micrococcus luteus , thiazole , stereochemistry , antimicrobial , docking (animal) , antibacterial activity , candida albicans , active site , staphylococcus epidermidis , enzyme , biochemistry , staphylococcus aureus , escherichia coli , bacteria , microbiology and biotechnology , organic chemistry , medicine , genetics , nursing , biology , gene
Synthesis, characterization and investigation of antimicrobial activity of 11 novel adamantanyl‐thiazoles are presented. Their structures were determined using 1 H and 13 C NMR, EI(+)‐MS, HRMS, and elemental analyses. Among the derivatives, compound 3c showed very strong activity, especially against Candida albicans ATCC 10231 and Candida parapsilosis ATCC 22019 with minimal inhibitory concentration (MIC) values ranging from 1.95 to 7.81 µg/ml. Compounds 3a and 3b showed good antifungal activity. Among the examined compounds, the widest spectrum of antibacterial activity possessed 3f that showed good activity, especially against Staphylococcus epidermidis ATCC 12228, Micrococcus luteus ATCC 10240, Bacillus subtilis ATCC 6633 with MIC values ranging from 31.25 to 62.5 µg/ml. Molecular docking studies of all compounds on the active sites of microbial enzymes indicated possible targets sterol 14 α ‐demethylase, secreted aspartic proteinase (SAP), N ‐myristoyltransferase (NMT), and topoisomerase II. Thiazoles 3a , 3b , 3c , 3d , 3e , 3f , 3g , 3h , 3i , 3j , 3k showed more favorable affinity to SAP and NMT than the native ligand.