Priprava i strukturna karakterizacija konjugata valinola s ferocen-karboksilnim kiselinama

master's thesis

• Title (english): Preparation and structural characterization of conjugates of valinol with ferrocene-carboxylic acids
• Author: Antonio Damjanović
• Mentor: Monika Kovačević (mentor)
• Committee member: Lidija Barišić (predsjednik povjerenstva)
• Committee member: Anita Horvatić (član povjerenstva)
• Committee member: Mojca Čakić Semenčić (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: 2024-12-17, Croatia
• Scientific / art field, discipline and subdiscipline: BIOTECHNICAL SCIENCES; Biotechnology

Abstract

Peptidomimetici predstavljaju skupinu spojeva koji kroz specifične strukturne modifikacije oponašaju sekundarne strukturne elemente prirodnih peptida. U ovom je radu pripravljena i konformacijski analizirana nova vrsta peptidomimetika, Ac−L−Val−NH−Fn−CO−O−CH₂−CH[CH(CH₃)₂]−NHBoc ferocenskih (13) i depsipeptida Ac−D−Val−NH−Fn−CO−O−CH₂− CH[CH(CH₃)₂]−NHBoc (14), izvedenih iz ferocenske aminokiseline i valinola. Glavni je cilj bio istražiti kako zamjena amidne veze esterskom utječe na konformacijski prostor i sekundarnu strukturu pripravljenih spojeva. Sintetizirani depsipeptidi analizirani su IR-, NMR- i CD-spektroskopijom kako bi se odredila njihova sposobnost formiranja intramolekulskih vodikovih veza. Rezultati su pokazali da zamjena amidne veze esterskom, koja reducira broj dostupnih donora vodikove veze, izravno utječe na obrazac intramolekulskih vodikovih veza. Temperaturno- i koncentracijski-ovisni spektri ukazali su na značajne promjene u obrascu vodikovih veza, u usporedbi s prije pripravljenim analozima koji nemaju estersku vezu. Ovaj rad doprinosi boljem razumijevanju konformacijskih svojstava ferocenskih depsipeptida i njihovog potencijala za razvoj novih bioaktivnih molekula.

Abstract (english)

Peptidomimetics represent a group of compounds that mimic the secondary structural elements of natural peptides through specific structural modifications. In this work, new peptidomimetics were prepared and conformationally analyzed: the ferrocene depsipeptides Ac−L−Val−NH−Fn−CO−O−CH₂−CH[CH(CH₃)₂]−NHBoc (13) and Ac−D−Val−NH−Fn−CO−O−CH₂− CH[CH(CH₃)2]−NHBoc (14), derived from ferrocene amino acid and valinol. The main goal was to investigate how the replacement of the amide bond by an ester bond affects the conformational space and 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. The results showed that replacing the amide bond with an ester reduces the number of available hydrogen bond donors, which directly affects the pattern of intramolecular hydrogen bonding. Temperature and concentration dependent spectra indicated significant changes in hydrogen bonding compared to previously prepared analogs without ester bonding. This work contributes to a better understanding of the conformational properties of ferrocene depsipeptides and their potential for the development of new bioactive molecules.

• Keywords: ferocen; peptidomimetici; konformacijska analiza; depsipeptidi; valinol
• Keywords (english): ferrocene; peptidomimetics; conformational analysis; depsipeptides; valinol
• Language: croatian
• URN:NBN: urn:nbn:hr:159:970573
• 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: 2025-01-29 09:33:52