Chemical compound libraries are big collections of many different chemical entities, which are normally used in high throughput screening with the intention of finding new hit
molecules in the drug discovery process. Different pharmaceutical companies have through the years of their existence each created large compound libraries either by synthesis of new chemical compounds and modification of the already existing structure, or by isolation from
different natural products.
Commercially available compound libraries are also available, but to create one from scratch, it would take several years to be completed. The answer to that could be click chemistry, which focuses on compounds that can be created by joining together different modular blocks. The joining of this blocks must be as simple as joining together a buckle. This requires simple, modular, broad chemical reactions which create easily removable side products. One of few suitable candidates is Huisgen 1,3-dipolar cycloaddition between an azide and alkyne which gives us a 1,4-triazole isomer in the presence of Cu(I) ions.
Within this master thesis we synthesized and purified several azide and dialkyne compounds which we later used to prepare different compound libraries with the help of click reactions.
In each of the click reactions azides reacted with one of the prepared dialkyne compounds. Each dialkyne could react with two different or two identical azide compounds which gave
us n2 (n=number of azides in click reaction) of different ditriazole compounds with each click reaction. Each click reaction represented a different compound library. Later we
confirmed the formation of ditriazole compounds with mass spectrometer. We also tested inhibitory properties of each prepared library on the MurA enzyme and minimal inhibitory
concentration (MIC) on E. coli and S. aureus bacteria. None of the three prepared chemical libraries showed any inhibitory activity against the selected enzyme or bacteria but that does
not exclude the possibility that one of the compounds inhibits some other enzyme.
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