Title Dizajn linearnih i cikličkih katalitičkih peptida
Title (english) Design of linear and cyclic catalytic peptides
Author Sabino Sepčić
Mentor Daniela Kalafatović (mentor)
Committee member Nela Malatesti (predsjednik povjerenstva)
Committee member Daniela Kalafatović (član povjerenstva)
Committee member Željko Svedružić (član povjerenstva)
Granter University of Rijeka (Faculty of Biotechnology and Drug Development) Rijeka
Defense date and country 2022-09-19, Croatia
Scientific / art field, discipline and subdiscipline INTERDISCIPLINARY AREAS OF KNOWLEDGE Biotechnology in Biomedicine (natural science, biomedicine and healthcare, bioethics area
Abstract Pozadina: Enzimi su proteini koji ubrzavaju kemijske reakcije stvaranjem povoljnih uvjeta za pretvorbu supstrata u produkte. Enzimi su velike makromolekule građene od aminokiselina povezanih peptidnim vezama. Peptidi, koji su također sastavljeni od aminokiselina, su manji i jednostavniji od proteina i mogu imati katalitička svojstva.
Cilj: Glavna svrha ovoga rada je istraživanje promjena svojstva katalize i samoorganizacije kod peptida koje proizlaze iz izmjena aminokiselina.
Metode: Tehnike koje su korištene su sinteza na čvrstom nosaču, tekuća kromatografija, masena spektrometrija, infracrvena spektroskopija, katalitički kinetički test i računalna simulacija molekularne dinamike.
Rezultati: Dva linearna i dva ciklička peptida su sintetizirana i karakterizirana. Strukture sintetiziranih peptida su kromatografski potvrđene što dokazuje mogućnost ciklizacije oktapeptida na čvrstom nosaču. Linearni peptidi formiraju supramolekularne strukture u obliku β-ploče sa cinkom. Daljnja analiza peptida sa katalitičkim kinetičkim testom je potrebna za dokazivanje njihovih katalitičkih svojstava.
Zaključak: Kombinacija računalnih i laboratorijskih tehnika je koristan alat u dizajnu peptida. Dizajn katalitičkih peptida relativno je novo polje proučavanja, stoga ovaj rad ima za cilj steći detaljnija saznanja o području.
Abstract (english) Background: Enzymes are proteins that help speed up chemical reactions by creating favourable environment for the conversion of substrates into products. Enzymes are large macromolecules composed of amino acids connected with peptide bonds. Peptides, which are also made up of amino acids, are smaller and easier to synthesize than proteins and can display catalytic properties.
Aim: The main purpose of this thesis is to explore the changing of self-assembly and catalytic properties of peptides by introducing amino acid alterations.
Methods: Techniques used are solid phase peptide synthesis, liquid chromatography, mass spectrometry, infrared spectroscopy, catalytic kinetic assay and computational molecular dynamics simulation.
Results: Two linear and two cyclic peptides were synthesized and characterized. The chromatography data validates the synthesized peptides which proves the possibility of octapeptide on-resin cyclization. Linear peptides formed supramolecular β-sheet-like structures with zinc. Further analysis of the peptides using the catalytic kinetic assay in needed to confirm their catalytic properties.
Conclusions: The combination of computational and laboratory techniques is a useful tool in peptide design. Catalytic peptide design is a newly emerging field of study and for this reason, this thesis aims to obtain a better understanding of the matter.
Keywords
Peptid
kataliza
dizajn peptida
ciklizacija
Keywords (english)
Peptide
catalysis
peptide design
cyclization
Language croatian
URN:NBN urn:nbn:hr:193:163367
Project Number: UIP-2019-04-7999 Title: Dizajn katalitički aktivnih peptida i peptidnih nanostruktura Title: Design of short catalytic peptides and peptide assemblies Acronym: DeShPet Leader: Daniela Kalafatović Jurisdiction: Croatia Funder: HRZZ Funding stream: UIP
Study programme Title: Medicinal chemistry Study programme type: university Study level: graduate Academic / professional title: magistar/magistra medicinske kemije (magistar/magistra medicinske kemije)
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Access conditions Open access Embargo expiration date: 2024-09-19
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Created on 2022-09-22 11:33:21