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master's thesis
Računalne simulacije kompleksa ljudske dipeptidil-peptidaze III s angiotenzinom-(1-7) i njegovim stabilnim analogom
Zagreb: University of Zagreb, Faculty of Science, 2018. urn:nbn:hr:217:300560
Čavka, Ivana
University of Zagreb
Faculty of Science
Department of Biology

Institutional repository: Repository of the Faculty of Science

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Čavka, I. (2018). Računalne simulacije kompleksa ljudske dipeptidil-peptidaze III s angiotenzinom-(1-7) i njegovim stabilnim analogom (Master's thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:300560

Čavka, Ivana. "Računalne simulacije kompleksa ljudske dipeptidil-peptidaze III s angiotenzinom-(1-7) i njegovim stabilnim analogom." Master's thesis, University of Zagreb, Faculty of Science, 2018. https://urn.nsk.hr/urn:nbn:hr:217:300560

Čavka, Ivana. "Računalne simulacije kompleksa ljudske dipeptidil-peptidaze III s angiotenzinom-(1-7) i njegovim stabilnim analogom." Master's thesis, University of Zagreb, Faculty of Science, 2018. https://urn.nsk.hr/urn:nbn:hr:217:300560

Čavka, I. (2018). 'Računalne simulacije kompleksa ljudske dipeptidil-peptidaze III s angiotenzinom-(1-7) i njegovim stabilnim analogom', Master's thesis, University of Zagreb, Faculty of Science, accessed 16 May 2024, https://urn.nsk.hr/urn:nbn:hr:217:300560

Čavka I. Računalne simulacije kompleksa ljudske dipeptidil-peptidaze III s angiotenzinom-(1-7) i njegovim stabilnim analogom [Master's thesis]. Zagreb: University of Zagreb, Faculty of Science; 2018 [cited 2024 May 16] Available at: https://urn.nsk.hr/urn:nbn:hr:217:300560

I. Čavka, "Računalne simulacije kompleksa ljudske dipeptidil-peptidaze III s angiotenzinom-(1-7) i njegovim stabilnim analogom", Master's thesis, University of Zagreb, Faculty of Science, Zagreb, 2018. Available at: https://urn.nsk.hr/urn:nbn:hr:217:300560

Metadata
TitleRačunalne simulacije kompleksa ljudske dipeptidil-peptidaze III s angiotenzinom-(1-7) i njegovim stabilnim analogom
Title (english)Computational Study of Complexes of Human Dipeptidyl Peptidase III with Angiotensin-(1-7) and its stabile analogue
AuthorIvana Čavka
MentorSanja Tomić (mentor)
MentorBiljana Balen (mentor)
Committee memberBiljana Balen (predsjednik povjerenstva)
Committee memberVesna Benković (član povjerenstva)
Committee memberDijana Škorić (član povjerenstva)
Committee memberInga Marijanović (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Biology)
Zagreb
Defense date and country2018-09-28, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Biology
Abstract
Dipeptidil-petidaza III (DPP III) je metalopeptidaza ovisna o cinku, koja ima široku supstratnu specifičnost. Uključena je u procese razgradnje kratkih peptida sastavljenih od tri do deset aminokiselina. Poznato je kako ljudska DPP III (hDPP III) posjeduje visok afinitet prema opioidnim peptidima i peptidima iz sustava renin-angiotenzin-aldosteron, pa se sukladno tome povezuje s različitim fiziološkim procesima kao što su regulacija krvnog tlaka, mehanizam modulacije boli i obrana od oksidacijskog stresa. Osim toga, aktivnost enzima DPP III se povezuje i s nekim patološkim stanjima kao što su pojava mrene i rast tumora. Ova otkrića razlog su tome što se DPP III razmatra kao potencijalna meta lijekova. Rad donosi rezultate molekulsko-dinamičkih (MD) simulacija enzima hDPP III u kompleksima s dva različita peptida. Prvi peptid je eksperimentalno potvrđen supstrat – angiotenzin-(1-7), a drugi peptid je njegov stabilizirani analog ACCA3, u kojem je valin zamijenjen neprirodnom cikličkom δ aminokiselinom (ACCA). Supstitucija valina onemogućuje degradaciju angiotenzina-(1-7) enzimom hDPP III. Rezultati rada otkrivaju moguće uzroke stabilnosti peptida ACCA3, a upućuju i na veću stabilnost kompleksa hDPP III s ACCA3 u odnosu na kompleks s angiotenzinom-(1-7).
Abstract (english)
Dipeptidyl peptidase III (DPP III) is a zinc-dependant metallopeptidase with a broad substrate specificity. It is involved in degradation of peptides with three to ten amino acid residues. It is known that human DPP III (hDPP III) exhibits high affinity to opioid peptides and peptides from renin-angiotensin-aldosteron system. In the view of this, hDPP III has been associated with different physiological processes, such as, pain-modulation, blood pressure regulation and, defence against oxidative stress. Furthermore, there have been some implications of hDPP III enzyme’s involvement in pathophysiological states like cataractogenesis and malignant growth. These findings have characterized DPP III as a potential drug target. This thesis brings results of molecular dynamics (MD) simulations of complexes of hDPP III with two different peptides. First one is angiotensin-(1-7), which has been experimentally confirmed as a substrate, and the other one is its stabile analogue ACCA3, in which valin has been substituted with a non-natural cyclic δ amino acid (ACCA). Valin substitution prevents angiotensin-(1-7) degradation by hDPP III. The results hold possible causes of ACCA3’s apparent stability and indicate the greater stability of the complex of hDPP III with ACCA3, than that of the complex of hDPP III with the angiotensin-(1-7).
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:300560
Study programmeTitle: Molecular Biology
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra molekularne biologije (magistar/magistra molekularne biologije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Embargo expiration date: 2020-09-28
Terms of useLicence In copyright icon
Created on2018-10-29 11:55:20