The need for alternative therapies becomes more pressing as bacterial infections become re-sistant to antibiotics. Peptides are considered nature’s antibiotic, as their mechanism of antimicro-bial activity either directly kills the infection or indirectly affects the host’s immune system. Peptoidsare a structural class of peptidomimetics, which are compounds that mimic natural peptides, whoseside-chain is appended to nitrogen instead of theα-carbon. This design prevents them from degra-dation by proteases. The future of peptidomimetics for drug design is promising as they are designedto contain specific physiochemical properties which allow for cell type selectivity. Antimicrobial ac-tivity is determined by many factors and applications of peptidomimetics. However, synthesis ofpeptoids possessing mainly the physiochemical properties of charge and hydrophobicity are inves-tigated. In this project, we synthesized two peptoids by the solid-phase sub-monomer method. Thesecond peptide allowed us to determine whether a structurally different peptoid required differentbromoacetylation and displacement times. HPLC-MS and an ÄKTA pure chromatography systemwere used to detect peptoid product and determine purity. It was determined that the original proto-col requires optimization of the the bromoacetylation and displacement steps, as our results suggestthat 20 minutes was optimal at both steps of peptoid synthesis.
|Uddannelser||Kemi, (Bachelor/kandidatuddannelse) Bachelor|
|Udgivelsesdato||17 dec. 2019|