Person:
TURAN, KADİR

Profile Picture

Email Address

Birth Date

Research Projects

Organizational Units

OrgUnit Logo
Organizational Unit

Job Title

Last Name

TURAN

First Name

KADİR

Name

Filters

2022 - 20232
Reset filters

Settings

Has files: true × Subject: Life Sciences ×

Search Results

Now showing 1 - 2 of 2
  • Thumbnail Image
    PublicationOpen Access
    Heterologous expression and initial in silico characterization of a novel snakin-Z peptide
    (2023-08-01) TURAN, KADİR; Teker T., Albayrak G., Turan K.
    Heterologous expression of the plant-derived snakin-Z (SNK-Z) peptide was carried out inEscherichia coliBL21 and Mach 1 strains using the pET14b, and pGEX-6P-1 vectors, and its tertiary structure was determined. The most efficient production of the recombinant fusion peptide (GST/SNK-Z) in both strains was achieved by induction with 0.1 mM isopropyl β-D-1-thiogalactopyranoside at 32°C. GST/SNK-Z with 30.14kDa which yielded 6.5mg/L protein, was purified by affinity chromatography followed by dialysis. The GST tags were removed using PreScission protease. The IC50of GST/SNK-Z was calculated as 12.07 µM forStaphylococcus aureus(ATCC 25923) using nonlinear regression analysis. The secondary structure of recombinant SNK-Z consisted of α-helix and coil sites. It’s 3-D model was generated with a confidence score of -0.20 and a template modeling score of 0.69 ± 0.12. The predicted solvent accessibility and B-factor profile were detected.This is the first report of heterologous expression of SNK-Z inE. coli. Our study provides fundamental data for the large-scale production of SNK-Z, which has a high potential for use in the pharmaceutical industry because of its previously reported antimicrobial effects.
  • Thumbnail Image
    PublicationOpen Access
    Effects of some interferon-related proteins on influenza a viruse RNA polymerase activity
    (2022-01-01) TURAN, KADİR; Çağlayan E., TURAN K.
    © 2022, Turkish Pharmacists Association. All rights reserved.Objectives: Interferons (IFNs) are one of the most important components of innate immunity against viruses, especially those carrying the RNA genomes such as influenza viruses. Upon viral infection, the IFNs are rapidly secreted, inducing the expression of several genes in the target cells and establishing an antiviral state. In this study, the effects of proteins encoded by some IFN-related genes on influenza A virus RNA-dependent RNA polymerase enzyme were investigated. We evaluated the importance of these proteins in the pathogenesis of different influenza A virus types. Materials and Methods: The IFN-related genes were amplified by polymerase chain reaction from the HEK293 cDNA library and cloned into pCHA expression vector. The expression of genes and subcellular localizations of the proteins were determined by Western blotting and immunofluorescence staining, respectively. The effects of IFNs-related proteins on virus RdRP enzyme were determined by influenza A virus mini-replicons. Results: The study revealed that the influenza A virus infections significantly altered the transcript level of the IFN-related CCL5, IFIT1, IFIT3, IFITM3, and OAS1 genes in HEK293 cells. It was determined that the alteration of the gene expression was also related to the virus type. The mini-replicon assays showed that the transient expression of CCL5, IFI27, OAS1, IFITM3, IFIT1, and IFIT3 have inhibitory effects on WSN and/or DkPen type virus RdRP enzymes. We observed that the proteins except OAS1 inhibited WSN type RdRP enzyme at a higher level than that of DkPen enzyme. Conclusion: It was concluded that influenza A virus infection significantly alters the IFN-related gene expression in the cells. Most of the proteins encoded from these genes showed an inhibitory effect on the virus RdRP enzymes in the HEK293 cells. The inhibition of the influenza virus RdRP with IFN-related proteins may be the result of direct or indirect interactions between the host proteins and the viral enzyme subunits.