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undergraduate thesis
Inhibicijsko djelovanje seskviterpena (β-kariofilena i karofilen oksida) na aktivnost acetilkolinesteraze
završni rad
Split: University of Split, Faculty of Chemistry and Technology, 2016. urn:nbn:hr:167:552735
Bodač, Antonija
University of Split
Faculty of Chemistry and Technology
Division of Chemistry

Institutional repository: Repository of the Faculty of chemistry and technology

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Bodač, A. (2016). Inhibicijsko djelovanje seskviterpena (β-kariofilena i karofilen oksida) na aktivnost acetilkolinesteraze : završni rad (Undergraduate thesis). Split: University of Split, Faculty of Chemistry and Technology. Retrieved from https://urn.nsk.hr/urn:nbn:hr:167:552735

Bodač, Antonija. "Inhibicijsko djelovanje seskviterpena (β-kariofilena i karofilen oksida) na aktivnost acetilkolinesteraze : završni rad." Undergraduate thesis, University of Split, Faculty of Chemistry and Technology, 2016. https://urn.nsk.hr/urn:nbn:hr:167:552735

Bodač, Antonija. "Inhibicijsko djelovanje seskviterpena (β-kariofilena i karofilen oksida) na aktivnost acetilkolinesteraze : završni rad." Undergraduate thesis, University of Split, Faculty of Chemistry and Technology, 2016. https://urn.nsk.hr/urn:nbn:hr:167:552735

Bodač, A. (2016). 'Inhibicijsko djelovanje seskviterpena (β-kariofilena i karofilen oksida) na aktivnost acetilkolinesteraze : završni rad', Undergraduate thesis, University of Split, Faculty of Chemistry and Technology, accessed 26 December 2024, https://urn.nsk.hr/urn:nbn:hr:167:552735

Bodač A. Inhibicijsko djelovanje seskviterpena (β-kariofilena i karofilen oksida) na aktivnost acetilkolinesteraze : završni rad [Undergraduate thesis]. Split: University of Split, Faculty of Chemistry and Technology; 2016 [cited 2024 December 26] Available at: https://urn.nsk.hr/urn:nbn:hr:167:552735

A. Bodač, "Inhibicijsko djelovanje seskviterpena (β-kariofilena i karofilen oksida) na aktivnost acetilkolinesteraze : završni rad", Undergraduate thesis, University of Split, Faculty of Chemistry and Technology, Split, 2016. Available at: https://urn.nsk.hr/urn:nbn:hr:167:552735

Metadata
TitleInhibicijsko djelovanje seskviterpena (β-kariofilena i karofilen oksida) na aktivnost acetilkolinesteraze : završni rad
Title (english)Inhibitory effect of sesquiterpenes (β-caryophyllene and caryophyllene oxide) on activity of acetylcholinesterase : bachelor thesis
AuthorAntonija Bodač
MentorFranko Burčul (mentor)
Committee memberFranko Burčul (predsjednik povjerenstva)
Committee memberMila Radan (član povjerenstva)
Committee memberMario Nikola Mužek (član povjerenstva)
GranterUniversity of Split
Faculty of Chemistry and Technology
(Division of Chemistry)
Split
Defense date and country2016-09-21, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
Acetilkolinesteraza (AChE) je enzim iz obitelji hidrolaza (E.C.3.1.1.7.). Razgrađuje neuroprijenosnik acetilkolin na acetat i kolin i tako smanjuje aktivnost acetilkolina. Inhibicija acetilkolinesteraze ima ključnu ulogu u ublaţavanju simptoma kod Alzheimerove demencije (vaţno za početne stadije). Alzheimerova bolest je progresivna degenerativna bolest središnjeg živčanog sustava koja se očituje gubitkom živčanih stanica u moždanoj kori s posljedičnom atrofijom mozga i progresivnom demencijom. Demencija je karakterizirana višestrukim kognitivnim deficitima koji uključuju gubitak sposobnosti pamćenja, razmišljanja, rasuđivanja i dr. Inhibitori kolinesteraza su danas jedina terapija za ublaţavanje simptoma Alzheimerove bolesti. Cilj ovog rada je bio ispitati sposobnost inhibicije enzima acetilkolinesteraze korištenjem seskviterpena (<i>β</i>-kariofilena i kariofilen oksida) kao inhibitora. <i>β</i>-kariofilen je pokazao dobru inhibicijsku sposobnost dok kariofilen oksid nije pokazao inhibicijsku aktivnost. Povećanjem koncentracije <i>β</i>-kariofilena raste i postotak inhibicije, a najveća vrijednost inhibicije postignuta je pri koncentraciji od 45,45 µg mL<sup>-1</sup> i iznosi 96,13 %, dok je IC<sub>50</sub> vrijednost iznosila 12,39 µg mL<sup>-1</sup>.
Abstract (english)
Acetylcholinesterase (AChE) is an enzyme that belongs to the hydrolases family (E.C.3.1.1.7.), it catalyses the hydrolysis of the neurotransmitter, acetylcholine, to acetate and choline. Inhibition of acetylcholinesterase has a crucial role in the treatment of Alzheimer's dementia (important at early stages). Alzheimer's disease is a progressive neurodegenerative disease of the central nervous system, which is manifested by a loss of nerve cells in the cerebral cortex of the brain resulting in atrophy and progressive dementia. Dementia is characterized by multiple cognitive deficits including loss of memory, judgement, ability, thinking and other. Cholinesterase inhibitors are still the only therapy for patients with Alzheimer's disease. The aim of this study was to examine the ability of sesquiterpenes (<i>β</i>-caryophyllene, caryophyllene oxide) to inhibit AChE. <i>β</i>-caryophyllene showed good inhibitory activity on AChE , while caryophyllene oxide showed no activity. It was concluded that β-caryophyllene showed ability to inhibit the AChE in concentration dependant manner. Maximum percentage of AChE inhibition of 96,13 %, was achieved at <i>β</i>-caryophyllene concentration of 45,45 µg mL<sup>-1</sup>, while IC<sub>50</sub> value was 12,39 µg mL<sup>-1</sup>.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:167:552735
ProjectNumber: 6897
Title: Istraživanje bioaktivnih spojeva iz dalmatinskog bilja: njihov antioksidacijski karakter i utjecaj na enzimsku inhibiciju i zdravlje
Acronym: BioActCom
Leader: Mladen Miloš
Jurisdiction: Croatia
Funder: HRZZ
Study programmeTitle: Chemistry
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) kemije (sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) kemije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
Public noteKljučne riječi doradio knjižničar / Key words have been revised by the librarian
Created on2017-06-07 12:21:12