Istraživanje supramolekulskih struktura tripeptida Phe-Phe-Ala infracrvenom spektroskopijom

master's thesis

• Title (english): Study of supramolecular structures of Phe-Phe-Ala tripetides by infrared spectroscopy
• Author: Ivana Paradžik
• Mentor: Leo Frkanec (mentor)
• Mentor: Snežana Miljanić (mentor)
• Committee member: Vesna Petrović Peroković (predsjednik povjerenstva)
• Committee member: Snežana Miljanić (član povjerenstva)
• Committee member: Željka Soldin (član povjerenstva)
• Committee member: Nives Galić (član povjerenstva)
• Granter: University of Zagreb; Faculty of Science; (Department of Chemistry); Zagreb
• Defense date and country: 2018-07-02, Croatia
• Scientific / art field, discipline and subdiscipline: NATURAL SCIENCES; Chemistry

Abstract

U ovom diplomskom radu sintetizirani su metilni ester i amid, N-acetiltripeptidi
aminokiselinskog slijeda L-fenilalanin-L-fenilalanin-L-alanin, koji se razlikuju prema
funkcijskoj skupini na C kraju peptida. Aminokiselinski slijed FFA je dio amiloida β za koji
je dokazano kako se nalazi u plakovima u mozgu pacijenata oboljelih od Alzheimerove
bolesti. Kao model samoorganiziranja molekula amiloida, oba tripeptida su upotrijebljena za
pripravu gelova u tri različita otapala, acetonitrilu, vodi i teškoj vodi. Infracrvenom
spektroskopijom istražile su se sekundarne strukture tripeptida u pripremljenim gelovima,
ponajprije analizom vrpce amid I u spektrima. Osim sekundarnih struktura, proučavana je i
morfologija niti gelskih struktura pomoću transmisijskog elektronskog mikroskopa.

Abstract (english)

In this graduate thesis, methyl ester and amide were synthesised, N-acetyltripeptides with LPhenylalanine-
L-Phenylalanine-L-Alanine sequence which differ depending on functional
group at the C end of the peptide. The amino acid sequence FFA is part of the amyloid β in
the brain plaques of patients with Alzheimer's disease. As a model of self-organization of the
amyloid molecule, both tripeptides were used for the gels preparation in three solvents,
acetonitrile, water and heavy water. Infrared spectroscopy was used to investigate the
secondary structures of the tripeptide in prepared gels, mainly by analysis of amide I band.
Also, gel morphology was studied usingtransmission electron microscopy.

• Keywords: Alzheimerova bolest; amiloid ß; infracrvena spektroskopija; samo-udruživanje u gelovima; supramolekulski gelovi; sekundarna struktura proteina; TEM
• Keywords (english): Alzheimer's disease; amyloid ß; infrared spectroscopy; protein secondary structure; self-assembled gels; supramolecular gels; TEM
• Language: croatian
• URN:NBN: urn:nbn:hr:217:280465
• Study programme: Title: Graduate university studies in chemistry; specializations in: Research programme; Course: Research programme; Study programme type: university; Study level: graduate; Academic / professional title: magistar/magistra kemije (magistar/magistra kemije)
• Type of resource: Text
• File origin: Born digital
• Access conditions: Open access; Embargo expiration date: 2020-07-02
• Created on: 2018-07-11 12:22:53