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master's thesis
Molekulsko modeliranje inhibicije kreatin kinaze
Osijek: Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, 2024. urn:nbn:hr:152:318578
Briševac, Tea
Josip Juraj Strossmayer University of Osijek
Faculty of Medicine Osijek

Institutional repository: Repository of the Faculty of Medicine Osijek

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Briševac, T. (2024). Molekulsko modeliranje inhibicije kreatin kinaze (Master's thesis). Osijek: Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek. Retrieved from https://urn.nsk.hr/urn:nbn:hr:152:318578

Briševac, Tea. "Molekulsko modeliranje inhibicije kreatin kinaze." Master's thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, 2024. https://urn.nsk.hr/urn:nbn:hr:152:318578

Briševac, Tea. "Molekulsko modeliranje inhibicije kreatin kinaze." Master's thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, 2024. https://urn.nsk.hr/urn:nbn:hr:152:318578

Briševac, T. (2024). 'Molekulsko modeliranje inhibicije kreatin kinaze', Master's thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, accessed 09 December 2024, https://urn.nsk.hr/urn:nbn:hr:152:318578

Briševac T. Molekulsko modeliranje inhibicije kreatin kinaze [Master's thesis]. Osijek: Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek; 2024 [cited 2024 December 09] Available at: https://urn.nsk.hr/urn:nbn:hr:152:318578

T. Briševac, "Molekulsko modeliranje inhibicije kreatin kinaze", Master's thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, Osijek, 2024. Available at: https://urn.nsk.hr/urn:nbn:hr:152:318578

Metadata
TitleMolekulsko modeliranje inhibicije kreatin kinaze
Title (english)Molecular modeling of creatine kinase inhibition
AuthorTea Briševac
MentorHrvoje Brkić (mentor)
Committee memberBarbara Viljetić (predsjednik povjerenstva)
Committee memberKatarina Mišković Špoljarić (član povjerenstva)
Committee memberHrvoje Brkić (član povjerenstva)
GranterJosip Juraj Strossmayer University of Osijek
Faculty of Medicine Osijek
Osijek
Defense date and country2024-07-16, Croatia
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Basic Medical Sciences
Abstract
Cilj istraživanja: Metodama molekulskog modeliranja ispitati inhibiciju kreatin kinaze, računski ispitati energijski najpovoljnije položaje inhibitora u enzimu i za energijski najpovoljnije položaje izračunati najbliže udaljenosti enzim-inhibitor. Nacrt studije: Istraživanje je napravljeno kao in silico studija – izgradnja računalnog modela enzima i inhibitora. Materijali i metode: Podaci o enzimu CK preuzeti su iz baze PDB, a podaci o tenofovir fosfatu su preuzeti iz PubChem baze. Za uklapanje je korišten web-server SwissDock. Sve strukture su vizualizirane korištenjem softvera VMD. Rezultati: Za sve ispitane točkaste mutacije u ovom istraživanju dobivena je negativna energija vezanja za TVF. Najnižu energiju vezanja su imale mutacije W211R, Y173C, I92H, R130H i N286I. Najpovoljniji energijski položaj nalaze se u blizini aminokiselinskih ostataka Arg130, Arg132, Arg236 i Glu232. Zaključak: Na temelju provedenog istraživanja možemo zaključiti da je za sve ispitane točkaste mutacije dobivena negativna energija vezanja. Najnižu energiju vezanja su imale mutacije R130H, R132C, W211R i N286I, stoga su najmanje aktivni.
Abstract (english)
Objectives: Using molecular modeling methods, analyse creatin kinase inhibition by examining the energetically favorable positions of the inhibitor and calculate the nearest enzyme-inhibitor distances for optimal energy efficiency. Study design: The research was done as an in silico study – building a computer model of enzymes and inhibitors. Materials and methods: CK enzyme data were taken from the PDB base and tenofovir phosphate data were taken from the PubChem base. SwissDock server was used for docking. All structures were visualized using VMD software. Results: Negative binding energy to TVF was obtained for all tested point mutations in this study. The lowest binding energy was spotted in mutations W211R, Y173C, I92H, R130H and N286I. The most favorable energy position is located near the amino acid residues Arg130, Arg132, Arg236 and Glu232. Conclusion: Based on the findings of the research, a conclusion can be drawn that in all mutations there was a decrease in activity. The lowest binding energy had the R130H, R132C, W211R and N286I mutations; therefore, they are the least active.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:152:318578
Study programmeTitle: University graduate study
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra medicinsko laboratorijske dijagnostike (magistar/magistra medicinsko laboratorijske dijagnostike)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2024-10-14 09:56:10