prikaz prve stranice dokumenta Structural and functional characterization of the hyaluronidase protein complex
Rad dostupan nakon 2026-11-19
diplomski rad
Structural and functional characterization of the hyaluronidase protein complex
2024. urn:nbn:hr:159:449445
Anđelini, Magdalena
Sveučilište u Zagrebu
Prehrambeno-biotehnološki fakultet
Zavod za kemiju i biokemiju
Laboratorij za biokemiju

Citirajte ovaj rad

Anđelini, M. (2024). Structural and functional characterization of the hyaluronidase protein complex (Diplomski rad). Zagreb: Sveučilište u Zagrebu, Prehrambeno-biotehnološki fakultet. Preuzeto s https://urn.nsk.hr/urn:nbn:hr:159:449445

Anđelini, Magdalena. "Structural and functional characterization of the hyaluronidase protein complex." Diplomski rad, Sveučilište u Zagrebu, Prehrambeno-biotehnološki fakultet, 2024. https://urn.nsk.hr/urn:nbn:hr:159:449445

Anđelini, Magdalena. "Structural and functional characterization of the hyaluronidase protein complex." Diplomski rad, Sveučilište u Zagrebu, Prehrambeno-biotehnološki fakultet, 2024. https://urn.nsk.hr/urn:nbn:hr:159:449445

Anđelini, M. (2024). 'Structural and functional characterization of the hyaluronidase protein complex', Diplomski rad, Sveučilište u Zagrebu, Prehrambeno-biotehnološki fakultet, citirano: 02.03.2025., https://urn.nsk.hr/urn:nbn:hr:159:449445

Anđelini M. Structural and functional characterization of the hyaluronidase protein complex [Diplomski rad]. Zagreb: Sveučilište u Zagrebu, Prehrambeno-biotehnološki fakultet; 2024 [pristupljeno 02.03.2025.] Dostupno na: https://urn.nsk.hr/urn:nbn:hr:159:449445

M. Anđelini, "Structural and functional characterization of the hyaluronidase protein complex", Diplomski rad, Sveučilište u Zagrebu, Prehrambeno-biotehnološki fakultet, Zagreb, 2024. Dostupno na: https://urn.nsk.hr/urn:nbn:hr:159:449445

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Podaci o radu
NaslovStructural and functional characterization of the hyaluronidase protein complex
Naslov (hrvatski)Strukturna i funkcionalna karakterizacija proteinskog kompleksa hijauronidaze
AutorMagdalena Anđelini
MentorIgor Stuparević (mentor)
Ustanova koja je dodijelila
akademski / stručni stupanj		Sveučilište u Zagrebu
Prehrambeno-biotehnološki fakultet
(Zavod za kemiju i biokemiju)
(Laboratorij za biokemiju)
Zagreb
Datum i država obrane2024-07-03, Hrvatska
Znanstveno / umjetničko
područje, polje i grana		BIOTEHNIČKE ZNANOSTI
Biotehnologija
Sažetak
The extracellular matrix (ECM) is a complex network of macromolecules that play essential structural and functional roles in tissue organization and the regulation of cellular processes. It undergoes continuous remodeling, primarily mediated by matrix metalloproteinases (MMPs), serine proteases (e.g., human neutrophil elastase, HNE), and hyaluronidases (Hyal). However, these enzymes also contribute to pathological tissue remodeling, leading to conditions such as inflammation, tumor progression,... Više and metastasis. Understanding their molecular characteristics and detailed mechanisms, and developing potential inhibitors is a significant challenge. Despite growing interest, there are only a few studies detailing their protein structures, spatial conformations, oligomerization, physicochemical properties (e.g., the exact pI value for Hyal), or the relationship between their catalytic activity and preparation/analysis conditions. Additionally, the literature lacks information regarding the quality or purity of samples used in catalytic and affinity assays, and the impact of sample quality on in vitro results. This internship project utilizes highly complementary analytical tools. Quality control by UHPLC-ESI-QTOF MS with online desalting and MALDI-TOF MS confirmed the good quality of HNE, MMP-1, and Hyal2 preparations but revealed that BTH is surprisingly impure. Proteomics assays even detected the presence of BSA in BTH samples. Native Liquid MALDI successfully characterized the oligomerization of HNE, MMP-1, and Hyal2. Results indicated that HNE does not form oligomers, MMP-1 forms dimers, and Hyal2 forms tetramers. Furthermore, a significant influence of a crowding agent (dextran 476 kDa) used to mimic the ECM on the inhibition of BTH by both natural and synthetic compounds was demonstrated by CE-UV catalytic assays and by MST affinity tests. This finding underscores the importance of studying proteins under conditions that closely resemble physiological environments. The innovative information collected during this internship will significantly advance studies on ECM targets. Sakrij dio sažetka
Ključne riječi
Jezikengleski
URN:NBNurn:nbn:hr:159:449445
Studijski programNaziv: Molekularna biotehnologija
Vrsta studija: sveučilišni
Stupanj studija: diplomski
Akademski / stručni naziv: magistar/magistra inženjer/inženjerka molekularne biotehnologije (mag. ing. biotechn.)
Vrsta resursaTekst
Način izrade datotekeIzvorno digitalna
Prava pristupaRad dostupan nakon
Datum isteka embarga: 2026-11-19
Uvjeti korištenjaIkona licence Zaštićeno autorskim pravom.
Datum i vrijeme pohrane2024-11-19 13:28:59
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