Browsing by Author "Şener, Azize"

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Citation - WoS: 1
Citation - Scopus: 1
A Comparative Study of Biochemical, Antimicrobial Effects and Phytochemical Composition Analysis of Glycyrrhiza Glabra L. Varieties Root Extracts
(Marmara University, 2025) Sen, Ali; Servı, Hüseyın; Barak, Timur Hakan; Tekin, Fethullah; Şener, Azize; Marzi, Mahdi; Gülmez, Gizem
Plants are the significant global interest as alternative treatment sources with their biologically activecompounds. This study compares the chemical composition and the antioxidant, antidiabetic, and antimicrobialproperties of ethanol extracts of G. glabra L. two different varieties from different regions. The phytochemicalcompositions was determined using GC-MS. Additionaly, total phenolic (TPC), flavonoid (TFC) and triterpene (TTC)contents were determined. Glycyrrhizic acid contents were analysed by HPLC. G. glabra var. glandulifera (GF1) showedthe highest antioxidant activity. All extracts had strong antidiabetic effects, besides GF1 showing the highest effect. TheMIC values was determined against 8 bacterial and 1 yeast strain and values ranged from 2.500 to 0.500; 2.500 to 0.714;2.500 to 0.714 for G. glabra var. glabra (GB), GF1, G. glabra var. glandulifera (GF2) respectively. Phytochemical studies haveshown that TPC was 100.60±5.06, 127.90±0.30, 69.01±0.30 mg GAE /g extract; TFC was 80.07±0.15, 25.35±0.0, 16.58±0.31mg KE/g and TTC was 217.30±6.05,172.40±2.17, 126.30±4.50 mg OE/g extract for GB, GF1, GF2, respectively. GF1 inparticular has the highest glycyrrhizic acid content. This study will contribute to the creation of new treatment strategiesand potential therapeutic agents in addition to the use of G. glabra L. in traditional treatments. Our study is also apreliminary study for future studies.
The Effect of Vitamin D and Paricalcitol on Protein Disulfide Isomerase
(Marmara University, 2025) Koksal, Murat; Şekerler, Turgut; Şener, Azize
Protein disulfide isomerase (PDI), a multifunctional protein plays an important role as oxidoreductase, isomerase and chaperone in the cell. Prior studies have identified PDI is highly expressed in many different cancer types and presented as a new potential target for cancer treatment. Here, we investigated vitamin D and its analogue paricalcitol in silico interaction of the human PDI and inhibition of PDI reductase activity in vitro. We observed a non-covalent mechanism where the main skeleton of the vitamin D3 ans paricalcitol sturcture is located at the hydrophobic site in the b' domain of PDI and forms a hydrogen bond with a residue (His138) in tihs domain. They also form multiple weak hydrophobic interactions with various chemical groups of the b' subunit. For the first time, we demonstrate that 1,25-dihydroxyvitamin D3 (1a,25(OH)2 vitamin D3) and paricalcitol inhibit the PDI reductase activity in vitro and their IC50 values are 20.79±1.43 nmol/L and 32.83±3.15 nmol/L respectively. The two compounds can also block the denistrosation activity of PDI.