Development of mimetic antimicrobial peptides and investigation of its effects

It is known that surfactin, which is an amphiphilic ring lipopeptide from the antimicrobial peptide (AMP) class, causes hole development and cell collapse by targeting the microbial cell membrane. Fermentation and purification of surfactin especially from Bacillus subtilis sources are critically important spets. In addition, after this biosynthesis process, the production of mimetic surfactin by biochemical synthesis the first stage of the study, a flow system was developed by synthesizing molecular imprinted polymers (MIP) that identify the lipophilic ends of surfactin to the metal-chelate structure containing carnitine as a ligand and embedded in the cryogel column, and then the separation and purification of ring surfactin from bio-extracts was investigated. In addition to the characterizations of these new separation materials, all developed by us, adsorption-desorption processes are also presented. In the second stage of the study, linear surfactin (L-surfactin) was obtained from the purified ring surfactin. The lipase-based cryogenic column system required for this was also produced for the first time in this study, and was used for the synthesis of L-surfactin and D-sorbitol-L-surfactin and F127 pluronic-L-surfactin mimetic AMP structures in a biochemical flow column and supported by characterization processes. In the third stage of the study, the usability of the produced circular and linear surfactin-based mimetic structures in bigel production and hydroxyapatite (HAp) synthesis was revealed and the findings obtained were supported by characterization. Finally, the antimicrobial effects of mimetic AMP structures prepared from the surfactin structures synthesized within the scope of the thesis were examined and discussed.