Analiza glikoproteina (gp) virusa zaire ebolavirus ter identifikacija potencialnih terapevtskih tarč z orodji probis in cmdock : diplomsko delo univerzitetnega študijskega programa I. stopnje

Poš, Aljoša

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Title:	Analiza glikoproteina (gp) virusa zaire ebolavirus ter identifikacija potencialnih terapevtskih tarč z orodji probis in cmdock : diplomsko delo univerzitetnega študijskega programa I. stopnje
Authors:	ID Poš, Aljoša (Author) ID Jukič, Marko (Mentor) More about this mentor... ID Bren, Urban (Comentor)
Files:	UN_Pos_Aljosa_2025.pdf (8,96 MB) MD5: D048F32B1B2FC24C0230AEA4C0A483FB
Language:	Slovenian
Work type:	Bachelor thesis/paper
Typology:	2.11 - Undergraduate Thesis
Organization:	FKKT - Faculty of Chemistry and Chemical Engineering
Abstract:	Zaire ebolavirus (EBOV) povzroča hemoragično mrzlico z visoko smrtnostjo in kljub napredku v medicinskih raziskavah še vedno nima odobrenega zdravila. V pričujočem diplomskem delu smo analizirali virusni glikoprotein (GP), ki ima osrednjo vlogo pri vstopu virusa v gostiteljske celice, z namenom identifikacije potencialnih zaviralcev. S pomočjo programske opreme ProBiS in PyMOL smo na osnovi strukturne podobnosti napovedali možna vezavna mesta na GP, ki bi lahko predstavljal terapevtsko tarčo. Na podlagi pregleda znanstvene literature smo oblikovali virtualno knjižnico malih molekul, ki smo jih nato z orodjem CmDock sidrali na izbrano, identificirano tarčno mesto. V nadaljevanju smo primerjali rezultate z digitalno knjižnico komercialno dostopnih spojin Enamin, pri čemer smo se osredotočili na analizo struktur spojin z najugodnejšimi ocenami sidranja. Izvedli smo kemoinformacijsko analizo strukturne podobnosti ter primerjavo osnovnih skeletov z znanimi zaviralci EBOV GP. Najobetavnejšim spojinam smo nato analizirali vezavne konformacije ter določili število in vrste nekovalentnih interakcij z GP. Ugotovili smo, da več spojin iz obeh knjižnic tvori potencialno stabilne komplekse z GP, pri čemer so nekatere spojine iz Enamin knjižnice po osnovni skeletni zgradbi presenetljivo podobne tistim iz naše strukturirane zbirke. Prav tako smo zaznali, da so nekatere spojine z najboljšimi CmDock ocenami sidranja kljub nizki Tanimotovi podobnosti vsebovale osnovne skeletne značilnosti že znanih zaviralcev. Slednje lahko uporabimo kot izhodišča za nadaljnje eksperimentalne raziskave na področju razvoja zaviralcev GP virusa EBOV.
Keywords:	Zaire ebolavirus, glikoprotein GP, zaviralci, vezavna mesta, molekulsko sidranje, strukturna podobnost
Place of publishing:	Maribor
Place of performance:	Maribor
Publisher:	[A. Poš]
Year of publishing:	2025
Number of pages:	1 spletni vir (1 datoteka PDF (XV, 98 f.))
PID:	20.500.12556/DKUM-93464
UDC:	577.112.85:004.762(043.2)
COBISS.SI-ID:	243651843
Publication date in DKUM:	10.07.2025
Views:	156
Downloads:	67
Metadata:
Categories:	KTFMB - FKKT
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Licences

License:	CC BY-NC-ND 4.0, Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International

Link:	http://creativecommons.org/licenses/by-nc-nd/4.0/
Description:	The most restrictive Creative Commons license. This only allows people to download and share the work for no commercial gain and for no other purposes.
Licensing start date:	27.06.2025

Secondary language

Language:	English
Title:	Analysis of the glycoprotein of zaire ebolavirus and identification of potential therapeutic targets using probis and cmdock tools
Abstract:	Zaire ebolavirus (EBOV) is the causative agent of hemorrhagic fever with high mortality, and despite advancements in medical research, no approved treatment is currently available. In this Bachelor thesis, we analyzed the viral glycoprotein (GP), which plays a central role in the viral entry into host cells, with the aim of identifying potential inhibitors. Using the software tools ProBiS and PyMOL, we predicted potential binding sites on GP based on structural similarity. Guided by a thorough review of the scientific literature, we constructed a virtual library of small molecules, which were subsequently docked into the identified target site using CmDock. To further evaluate the results, we compared them with a commercially available compound library from Enamine, focusing on the structural analysis of the top-scoring compounds. Through cheminformatics methods, we assessed the structural similarity and core scaffolds in comparison to known EBOV GP inhibitors. The most promising compounds were then subjected to binding conformation analysis with EBOV GP. Our findings indicate that several compounds from both libraries form potentially stable complexes with GP, with some Enamin compounds exhibiting a surprisingly high degree of core scaffold similarity to those in our curated library. Moreover, we observed that many top-ranked compounds from our virtual screening, despite relatively low Tanimoto similarity values, share key scaffold features with known GP inhibitors. These results provide a valuable basis for further experimental research aimed at developing novel inhibitors of the EBOV glycoprotein.
Keywords:	Zaire ebolavirus, glycoprotein GP, inhibitors, molecular docking, binding sites, structural similarity

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