20.500.12556/DKUM-97738 In silico načrtovanje potencialnih peptidov, ki preprečujejo agregacijo biofarmacevtskih proteinov diplomsko delo univerzitetnega študijskega programa I. stopnje In silico design of potential peptides that prevent the aggregation of biopharmaceutical proteins V diplomskem delu prikazujemo pristop in silico načrtovanja peptidov, ki bi lahko preprečevali agregacijo biofarmacevtskih proteinov. Namen našega dela je bil analizirati fizikalno-kemijske lastnosti več tisoč kratkih peptidnih sekvenc in oceniti njihov potencial za zaviranje agregacije. Osredotočili smo se na težke in lahke verige (s skupno več kot 7000 sekvenc dolžine 15 aminokislin), kjer smo kvantitativno izračunali vsebnost polarnih, nabitih, hidrofobnih in aromatskih aminokislin ter njihove deleže. Uporabili smo orodji CamSol Intrinsic in Aggrescan, s katerima smo ocenili topnost in agregacijski potencial posameznih zaporedij. Rezultati kažejo, da peptidi z višjo vsebnostjo polarnih in nabitih ostankov dosegajo višje CamSol ocene in nižje NHSA vrednosti, kar nakazuje na boljšo topnost in manjšo nagnjenost k agregaciji. Nasprotno pa je večja vsebnost hidrofobnih in aromatskih aminokislin korelirala z nižjo topnostjo in večjim agregacijskim potencialom. Izvedli smo tudi primerjave med težkimi in lahkimi verigami ter analizirali podobnosti zaporedij in lokalni prispevek posameznih aminokislin k topnosti. Diplomsko delo tako ponuja temelje za nadaljnje načrtovanje funkcionalnih peptidov, ki bi lahko služili kot terapevtska orodja za izboljšanje stabilnosti biofarmacevtskih produktov. This thesis presents an in silico approach to the design of peptides that may prevent the aggregation of biopharmaceutical proteins. The aim of our work was to analyze the physicochemical properties of thousands of short peptide sequences and evaluate their potential to inhibit aggregation. We focused on heavy and light chains (with over 7000 sequences, each 15 amino acids long), where we quantitatively calculated the number and proportion of polar, charged, hydrophobic, and aromatic amino acids. We used CamSol Intrinsic and Aggrescan tools to assess the solubility and aggregation propensity of individual sequences. The results show that peptides with a higher content of polar and charged residues achieved higher CamSol scores and lower NHSA values, indicating better solubility and a lower tendency to aggregate. Conversely, increased hydrophobic and aromatic amino acid content correlated with reduced solubility and higher aggregation potential. We also compared heavy and light chain sequences and analyzed sequence similarities, as well as the local contribution of individual amino acids to solubility. This thesis provides a foundation for further rational design of functional peptides that could serve as therapeutic tools for improving the stability of biopharmaceutical products. in silico načrtovanje agregacija proteinov antiagregacijski peptidi CamSol Aggrescan topnost peptidov in silico design protein aggregation anti-aggregation peptides CamSol Aggrescan peptide solubility true true false [E. Ristevska] Slovenski jezik Angleški jezik Diplomsko delo/naloga 2026-04-08 22:54:32 2026-04-24 12:43:17 2026-05-06 03:07:01 0000-00-00 00:00:00 2026 0 Maribor 0 Maribor 1 spletni vir (1 datoteka PDF (XI, 26 str.)) 0000-00-00 NiDoloceno NiDoloceno NiDoloceno 0000-00-00 0000-00-00 0000-00-00 547.466.1:544.77.051.2(043.2) 277050371 UN_Ristevska_Emilija_2026.pdf UN_Ristevska_Emilija_2026.pdf 1 D8E9C0C336CFA76A587923BB9F24FF85 c75ef8392f980bbf1b061b57ae19fd38ae5f103fcd831e199df4e62e99ea3166 f4d5caef-3ee7-11f1-a8d8-00155d0001a1 https://dk.um.si/Dokument.php?lang=slv&id=205573 Fakulteta za kemijo in kemijsko tehnologijo 0 0 0