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master's thesis
Molekulsko modeliranje enzima laktat dehidrogenaze-B i njegovih liganda kao kandidata za antikancerogene terapije
2024. urn:nbn:hr:152:577325
Sajda, Tamara
Josip Juraj Strossmayer University of Osijek
Faculty of Medicine Osijek

Cite this document

Sajda, T. (2024). Molekulsko modeliranje enzima laktat dehidrogenaze-B i njegovih liganda kao kandidata za antikancerogene terapije (Master's thesis). Osijek: Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek. Retrieved from https://urn.nsk.hr/urn:nbn:hr:152:577325

Sajda, Tamara. "Molekulsko modeliranje enzima laktat dehidrogenaze-B i njegovih liganda kao kandidata za antikancerogene terapije." Master's thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, 2024. https://urn.nsk.hr/urn:nbn:hr:152:577325

Sajda, Tamara. "Molekulsko modeliranje enzima laktat dehidrogenaze-B i njegovih liganda kao kandidata za antikancerogene terapije." Master's thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, 2024. https://urn.nsk.hr/urn:nbn:hr:152:577325

Sajda, T. (2024). 'Molekulsko modeliranje enzima laktat dehidrogenaze-B i njegovih liganda kao kandidata za antikancerogene terapije', Master's thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, accessed 31 October 2024, https://urn.nsk.hr/urn:nbn:hr:152:577325

Sajda T. Molekulsko modeliranje enzima laktat dehidrogenaze-B i njegovih liganda kao kandidata za antikancerogene terapije [Master's thesis]. Osijek: Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek; 2024 [cited 2024 October 31] Available at: https://urn.nsk.hr/urn:nbn:hr:152:577325

T. Sajda, "Molekulsko modeliranje enzima laktat dehidrogenaze-B i njegovih liganda kao kandidata za antikancerogene terapije", Master's thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, Osijek, 2024. Available at: https://urn.nsk.hr/urn:nbn:hr:152:577325

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Metadata
TitleMolekulsko modeliranje enzima laktat dehidrogenaze-B i njegovih liganda kao kandidata za antikancerogene terapije
Title (english)Molecular modeling of the enzyme lactate dehydrogenase-B and its ligands as candidates for anticancer therapies
AuthorTamara Sajda
MentorHrvoje Brkić (mentor)
Committee memberKatarina Mišković Špoljarić (predsjednik povjerenstva)
Committee memberBarbara Viljetić (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 i prikazati inhibiciju enzima laktat dehidrogenaze, ispitati energetski najpovoljnije položaje određenih liganda u enzimu te ispitati vezanje različitih liganda (tukatinib, kapmatinib i AXKO-0046) s navedenim enzimom. Nacrt studije: Istraživanje je napravljeno kao in silico studija – izgradnja računalnog modela enzima i inhibitora Materijali i metode: Podaci o enzimu LDH-B preuzeti su baze PDB, a podaci o inhibitorima tukatinib, kapmatinib i AXKO-0046 preuzeti su iz baze PubChem. Za predikciju energijski najpovoljnijeg položaja korišten je server LeDock. Sve strukture vizualizirane su korištenjem softvera VMD. Rezultati: Rezultati dobiveni korištenjem servera LeDock prikazuju energetski najpovoljnije konformacije inhibitora prilikom vezanja za aminokiselinske ostatke enzima. Ti rezultati su vizualizirani softverom VMD gdje je provedena ručna analiza interakcija inhibitora i enzima, mjereći njihovu udaljenost u angstremima. Zaključak: Računalnim metodama uklapanja dobiveni su energijski najpovoljniji položaji inhibitora tukatinib, kapmatinib i AXKO-0046. Najpovoljniji položaj inhibitora tukatinib je u veznim mjestima Ala96 i Asp52, najpovoljniji položaj inhibitora kapmatinib je u veznim mjestima Arg99 i Asp52, a najpovoljniji položaj inhibitora AXKO-0046 je u veznim mjestima Arg99 i Asp52.
Abstract (english)
Objectives: Using molecular modeling methods to examine and show the inhibition of the lactate dehydrogenase enzyme, to examine the most energy - efficient positions of certain ligands in the enzyme, and to examine the binding of different ligands (tucatinib, capmatinib and AXKO-0046) with enzyme. Study design: The research was done as an in silico study - building a computer model of enzymes and inhibitors. Materials and methods: Data on the enzyme LDH-B were taken from the PDB database, and data on the inhibitors tucatinib, capmatinib and AXKO-0046 were taken from the PubChem database. The LeDock server is used to predict the most energy - efficient position. All structures were visualized using VMD software. Results: The results obtained using the LeDock server show the most energy - efficient conformations of the inhibitor when binding to amino acid residues of the enzyme. These results were visualized with the VMD software, where a manual analysis of inhibitor-enzyme interactions was performed, measuring their distance in angstroms. Conclusion: The most energy - efficient positions of the inhibitors tucatinib, capmatinib and AXKO-0046 were obtained by molecular docking methods. The most energy - efficient position of the inhibitor tukatinib is in the binding sites Ala96 and Asp52, the most energy - efficient position of the inhibitor capmatinib is in the binding sites Arg99 and Asp52 and the most energy - efficient position of the inhibitor AXKO-0046 is in the binding sites Arg99 and Asp52.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:152:577325
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 10:00:44