Priprava i konformacijska analiza ferocenskih depsipeptida s alaninom i leucinom

master's thesis

• Title (english): Synthesis and conformational analysis of ferocene depsipeptides with alanine and leucine
• Author: Leona Galić
• Mentor: Monika Kovačević (mentor)
• Committee member: Lidija Barišić (predsjednik povjerenstva)
• Committee member: Antonela Ninčević Grassino (član povjerenstva)
• Committee member: Anita Horvatić (član povjerenstva)
• Granter: University of Zagreb; Faculty of Food Technology and Biotechnology; (Department of Chemistry and Biochemistry); (Laboratory for Organic Chemistry); Zagreb
• Defense date and country: 2025-01-24, Croatia
• Scientific / art field, discipline and subdiscipline: BIOTECHNICAL SCIENCES; Biotechnology

Abstract

Ferocenski biokonjugati s aminokiselinama često se koriste kao peptidomimetici. Uvođenje ferocenskog kalupa u peptidne lanace inducira tvorbu intermolekulskih vodikovih veza što omogućava nastanak različitih elemenata sekundarne strukture poput okreta, uzvojnica i β-ploča o čemu ovisi funkcija samog peptida. Jedna od neistraženih modifikacija ferocenskih peptidomimetika je zamjena jedne amidne veze esterskom vezom s ciljem priprave depsipeptida. Depsipeptidi, u odnosu na peptide, pokazuju veću otpornost prema enzimskoj degradaciji, povećanu specifičnost te konformacijske izmjene koje se odražavaju na karakter vodikovih veza i fleksibilnost. U sklopu ovog diplomskog rada pripravljeni su spojevi Ac–D–Leu–NH–FnCO−O−CH₂−CH[CH₂CH(CH₃)₂]−NHBoc (7) i Ac–D–Ala–NH–Fn–CO−O−CH₂−CH[CH₂CH(CH₃)₂]−NHBoc (11) kako bi se ispitao utjecaj zamjene jedne amidne veze esterskom vezom na obrazac i brojnost vodikovih veza i utjecaj na tvorbu elemenata sekundarne strukture pripravljenih spojeva. Sintetizirani depsipeptidi analizirani su IR-, NMR- i CD-spektroskopijom kako bi se odredila njihova sposobnost formiranja intramolekulskih vodikovih veza.

Abstract (english)

Ferrocene bioconjugates, which contain amino acids, are often used as peptidomimetics. The introduction of ferrocene favors the formation of intermolecular hydrogen bonds, and its insertion into peptide chains allows the formation of various secondary structural elements such as turns, coils and surfaces, on which the function of the peptide itself depends. One of the still unexplored modifications of ferrocene peptides is the replacement of an amide bond by an ester bond with the aim of producing the depsipeptides. Compared to peptides, depsipeptides exhibit greater resistance to enzymatic degradation, higher specificity and conformational changes that reflect the character of hydrogen bonds and flexibility. In this work, the compounds Ac–D–Leu–NH–Fn–CO−O−CH₂−CH[CH₂CH(CH₃)₂]−NHBoc (7) and Ac–D–Ala–NH–Fn–CO−O−CH₂−CH[CH₂CH(CH₃)₂]−NHBoc (11) were synthesized to investigate the effects of replacing an amide bond with an ester bond on the pattern and number of hydrogen bonds and the effects on the formation of elements of the secondary structure of the synthesized compounds. The synthesized depsipeptides were analyzed by IR, NMR and CD spectroscopy to determine their ability to form intramolecular hydrogen bonds.

• Keywords: ferocen; peptidomimetici; depsipeptidi; alanin; leucin; konformacijska analiza
• Keywords (english): ferocene; peptidomimetics; depsipeptides; alanine; leucine; conformational analysis
• Language: croatian
• URN:NBN: urn:nbn:hr:159:131587
• Study programme: Title: Molecular Biotechnology; Study programme type: university; Study level: graduate; Academic / professional title: magistar/magistra inženjer/inženjerka molekularne biotehnologije (magistar/magistra inženjer/inženjerka molekularne biotehnologije)
• Type of resource: Text
• File origin: Born digital
• Access conditions: Open access
• Created on: 2025-01-28 14:31:13