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undergraduate thesis
Molekulsko modeliranje enzima lipaze B i njegovih liganada
2024. urn:nbn:hr:152:521492
Diklić, Bruno
Josip Juraj Strossmayer University of Osijek
Faculty of Medicine Osijek

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Diklić, B. (2024). Molekulsko modeliranje enzima lipaze B i njegovih liganada (Undergraduate thesis). Osijek: Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek. Retrieved from https://urn.nsk.hr/urn:nbn:hr:152:521492

Diklić, Bruno. "Molekulsko modeliranje enzima lipaze B i njegovih liganada." Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, 2024. https://urn.nsk.hr/urn:nbn:hr:152:521492

Diklić, Bruno. "Molekulsko modeliranje enzima lipaze B i njegovih liganada." Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, 2024. https://urn.nsk.hr/urn:nbn:hr:152:521492

Diklić, B. (2024). 'Molekulsko modeliranje enzima lipaze B i njegovih liganada', Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, accessed 19 November 2024, https://urn.nsk.hr/urn:nbn:hr:152:521492

Diklić B. Molekulsko modeliranje enzima lipaze B i njegovih liganada [Undergraduate thesis]. Osijek: Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek; 2024 [cited 2024 November 19] Available at: https://urn.nsk.hr/urn:nbn:hr:152:521492

B. Diklić, "Molekulsko modeliranje enzima lipaze B i njegovih liganada", Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Faculty of Medicine Osijek, Osijek, 2024. Available at: https://urn.nsk.hr/urn:nbn:hr:152:521492

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Metadata
TitleMolekulsko modeliranje enzima lipaze B i njegovih liganada
Title (english)Molecular modeling of the lipase B enzyme and its ligands
AuthorBruno Diklić
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 country2024-09-19, Croatia
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Basic Medical Sciences
Abstract
Cilj istraživanja: Metodama molekulskog modeliranja ispitati inhibiciju lipaze B, ispitati energijski najpovoljnije položaje inhibitora u enzimu i ispitati vezanje različitih liganada s navedenim enzimom. Nacrt studije: Istraživanje je napravljeno kao in silico studija – izgradnja računalnog modela enzima i inhibitora. Materijali i metode: Podaci o enzimu lipaze B preuzeti su iz baze PDB, a podaci o ružmarinskoj kiselini, epikatehinu i epikatehin galatu preuzeti su iz baze PubChem. Za predviđanje najpovoljnijeg energijskog položaja korišten je softver LeDock. Sve molekule su vizualizirane u programu VMD. Rezultati: Rezultati najpovoljnijeg položaja vezanja inhibitora za enzim Lipazu B, prvo je korištena metoda uklapanja nakon čega su izmjerene sve međusobne udaljenosti inhibitora i enzima kraće od 3 Å. Zaključak: Metodom uklapanja dobiveno je da se inhibitori najviše vežu za aminokiselinske ostatke Gly, Pro, Asp, Thr te da je najpovoljnija energija vezanja u rješenju C1, a najmanja udaljenost enzima i inhibitora je u rješenju A2 na veznom mjestu Pro17.
Abstract (english)
Objectives: Using molecular modeling methods, investigate the inhibition of lipase B, examine the energetically most favorable positions of inhibitors within the enzyme, and analyze the binding of various ligands with the enzyme. Study design: The research was conducted as an in silico study, involving the construction of a computational model of the enzyme and inhibitors. Materials and methods: The data on the lipase B enzyme were obtained from the PDB database, while the data on rosmarinic acid, epicatechin, and epigallocatechin gallate were obtained from the PubChem database. The software LeDock was used to predict the most favorable energetic positions. All molecules were visualized using the VMD program. Results: The results for the most favorable binding position of the inhibitors to the lipase B enzyme were first obtained using the docking method, after which all distances between the inhibitors and the enzyme shorter than 3 Å were measured. Conclusion: Using the docking method, it was determined that inhibitors bind most strongly to the amino acid residues Gly, Pro, Asp, and Thr, with the most favorable binding energy in solution C1, while the shortest distance between the enzyme and the inhibitor is in solution A2 at the Pro17 binding site.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:152:521492
Study programmeTitle: University undergraduate study
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni prvostupnik/prvostupnica (baccalaureus/ baccalaurea) medicinske laboratorijske dijagnostike (sveučilišni prvostupnik/prvostupnica (baccalaureus/ baccalaurea) medicinske laboratorijske dijagnostike)
Type of resourceText
File originBorn digital
Access conditionsOpen access
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Created on2024-11-08 10:59:11