diplomsko delo
Tinkara Butara (Author), Marko Novinec (Mentor)

Abstract

Cilj diplomske naloge je bila identifikacija proteinskih tarč derivata hidroksinaftojske kisline (1-hidroksi-2-naftojske kisline), majhne biološko aktivne molekule. Spojina ima predhodno dokazano zaviralen učinek na rast bakterije Staphylococcus aureus, iskanje in identifikacija njenih proteinskih tarč pa je ključna za razumevanje molekularnih mehanizmov njenega protibakterijskega učinka. Z uporabo afinitetne kromatografije smo uspeli zaznati približno 25 kDa velik protein, ki se veže na ligand N-(4-aminobutil)-1-hidroksi-2-naftamid. Sledila je izolacija in analiza s pomočjo masne spektrometrije (MS). Kot potencialno tarčo naše male molekule smo identificirali NAD(P)H dehidrogenazo (kinon), znano tudi pod imenom WrbA. Encim ima ključno vlogo v dihalni verigi bakterijske celice, kjer ohranja ravnovesje v redoks procesih in aktivno sodeluje pri nastajanju mikrobnega biofilma. Te pomembne funkcije ga postavljajo v jedro bakterijskega odziva na stres. Blokiranje ali inhibicija delovanja NAD(P)H dehidrogenaze se zato zdi obetaven pristop za razvoj spojin s protimikrobnim delovanjem.

Keywords

proteinske tarče;protibakterijsko delovanje;hidroksinaftojska kislina;NAD(P)H dehidrogenaza (kinon);WrbA;diplomska dela;

Data

Language: Slovenian
Year of publishing:
Typology: 2.11 - Undergraduate Thesis
Organization: UL FKKT - Faculty of Chemistry and Chemical Technology
Publisher: [T. Butara]
UDC: 577.112(043.2)
COBISS: 195790083 Link will open in a new window
Views: 56
Downloads: 13
Average score: 0 (0 votes)
Metadata: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Other data

Secondary language: English
Secondary title: Identification of protein targets of hydroxynaphthoic acid derivatives with antibacterial activity
Secondary abstract: We investigated the identification of a protein target using the hydroxynaphthoic acid ligand (1-hydroxi-2-naphthoic acid), a small biologically active molecule. The compound has shown antimicrobial properties against Staphylococcus aureus in previous studies, underscoring the importance of discovering and characterizing its protein targets to gain insights into the mechanisms underlying its therapeutic effect. Using affinity chromatography, we were able to detect a protein of approximately 25 kDa that binds to the ligand N-(4-aminobutyl)-1-hydroxy-2-naphthamide. This was followed by isolation and analysis by mass spectrometry (MS). We succeeded in identifying NAD(P)H dehydrogenase (quinone), also known as WrbA, as a potential target of our small molecule. The enzyme plays a key role in the respiratory chain of the bacterial cell, where it maintains the balance of redox processes and is actively involved in the formation of a microbial biofilm. These crucial functions make it the centerpiece of the bacterial stress response. Blocking or inhibiting the action of NAD(P)H dehydrogenase therefore appears to be a promising approach for antimicrobial activity.
Secondary keywords: protein targets identification;antibacterial activity;hydroxynaphthoic acid;NAD(P)H dehydrogenase (quinone);Beljakovine;Univerzitetna in visokošolska dela;
Type (COBISS): Bachelor thesis/paper
Study programme: 1000371
Embargo end date (OpenAIRE): 1970-01-01
Thesis comment: Univ. v Ljubljani, Fak. za kemijo in kemijsko tehnologijo, UNI Biokemija
Pages: 1 spletni vir (1 datoteka PDF (37 str.))
ID: 23649479