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master's thesis
Simulacije molekulske dinamike kompleksa ljudske dipeptidil-peptidaze III s inhibitorima
Zagreb: University of Zagreb, Faculty of Science, 2016. urn:nbn:hr:217:692350
Tir, Nora
University of Zagreb
Faculty of Science
Department of Chemistry

Institutional repository: Repository of the Faculty of Science

Cite this document

Tir, N. (2016). Simulacije molekulske dinamike kompleksa ljudske dipeptidil-peptidaze III s inhibitorima (Master's thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:692350

Tir, Nora. "Simulacije molekulske dinamike kompleksa ljudske dipeptidil-peptidaze III s inhibitorima." Master's thesis, University of Zagreb, Faculty of Science, 2016. https://urn.nsk.hr/urn:nbn:hr:217:692350

Tir, Nora. "Simulacije molekulske dinamike kompleksa ljudske dipeptidil-peptidaze III s inhibitorima." Master's thesis, University of Zagreb, Faculty of Science, 2016. https://urn.nsk.hr/urn:nbn:hr:217:692350

Tir, N. (2016). 'Simulacije molekulske dinamike kompleksa ljudske dipeptidil-peptidaze III s inhibitorima', Master's thesis, University of Zagreb, Faculty of Science, accessed 04 January 2025, https://urn.nsk.hr/urn:nbn:hr:217:692350

Tir N. Simulacije molekulske dinamike kompleksa ljudske dipeptidil-peptidaze III s inhibitorima [Master's thesis]. Zagreb: University of Zagreb, Faculty of Science; 2016 [cited 2025 January 04] Available at: https://urn.nsk.hr/urn:nbn:hr:217:692350

N. Tir, "Simulacije molekulske dinamike kompleksa ljudske dipeptidil-peptidaze III s inhibitorima", Master's thesis, University of Zagreb, Faculty of Science, Zagreb, 2016. Available at: https://urn.nsk.hr/urn:nbn:hr:217:692350

Metadata
TitleSimulacije molekulske dinamike kompleksa ljudske dipeptidil-peptidaze III s inhibitorima
Title (english)Molecular dynamics simulations of complexes of human dipeptidyl peptidase III with inhibitors
AuthorNora Tir
MentorMarko Močibob (mentor)
MentorSanja Tomić (mentor)
Committee memberMarko Močibob (predsjednik povjerenstva)
Committee memberSanja Tomić (član povjerenstva)
Committee memberZlatko Mihalić (član povjerenstva)
Committee memberIvica Đilović (član povjerenstva)
Committee memberJosip Požar (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Chemistry)
Zagreb
Defense date and country2016-06-20, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
Dipeptidil-peptidaza III (DPP III) je o cinku ovisna peptidaza koja katalizira hidrolizu druge peptidne veze s N-kraja svojih supstrata. Enzim je široke supstratne specifičnosti, nepoznate osnovne fiziološke uloge, široke zastupljenosti među organizmima te prepoznatih uloga u procesima od interesa za razvoj lijekova. U ovom radu provedene su simulacije molekulske dinamike kompleksa ljudske DPP III s dvama inhibitorima za koje su poznati postotci inhibicije u odnosu na sintetski supstrat Arg-Arg-2-naftilamid. Za simulacije su korištene dvije konformacije enzima različite kompaktnosti kako bi se, računima slobodne energije vezanja, utvrdilo koja je povoljnija za vezanje liganda i upoznale interakcije liganda s aminokiselinskim ostatcima te cinkovim ionom u aktivnom mjestu. Dobiveni rezultati mogli bi poslužiti u daljnjem razvoju i testiranju potencijalnih inhibitora ovog enzima.
Abstract (english)
Dipeptidyl peptidase III (DPP III) is a zinc dependent peptidase which catalyses hydrolysis of the second N-terminal peptide bond of its substrates. DPP III is an enzyme of broad substrate specificity and it has been found in many organisms. Although its fundamental physiological role is unknown, it has been recognised in several processes of interest for the drug development. In this thesis, molecular dynamic simulations were done for the complexes of human DPP III with two inhibitors for which the percentages of inhibition have been measured for the Arg-Arg-2-naphthylamide synthetic substrate hydrolysis. Two enzyme conformations of different compactness were used for the simulations. Subsequently, the binding free energies were calculated in order to find out which one is more favorable for ligand binding and to obtain an insight into the ligand-protein interactions. The obtained results might be useful in future development and testing of potential inhibitors of this enzyme.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:692350
Study programmeTitle: 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 resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2017-01-27 10:57:17