Browsing by Subject "Neurodegenerative diseases"
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Item Turkish adaptation of Parkinson fatigue scale and investigating its psychometric properties(Lippincott Williams and Wilkins, 2019) Çilga G.; Genç A.; Çolakoǧlu B.D.; Kahraman T.Parkinson's disease (PD) is one of the most common chronic degenerative diseases of the nervous system. In PD, nonmotor symptoms are seen as frequently as motor symptoms. Fatigue can occur in all stages of PD and leads to significant disabilities. The aim of this study was to investigate the psychometric properties of the Turkish version of Parkinson fatigue scale (PFS). Ninety-six patients with idiopathic PD were included in this study with a cross-sectional and test-retest design. Structural validity, internal consistency and test-retest reliability of PFS were analyzed. For convergent validity, fatigue severity scale and modified fatigue impact scale were used. Internal consistency was determined by the Cronbach's α coefficient. For test-retest reliability, PFS was repeated after a 7-14-day period. Significant strong correlations were found between the PFS and the fatigue severity scale (r s =0.844) and the modified fatigue impact scale (r s =0.764), which indicate a high convergent validity. The Cronbach's α coefficient, which indicates the internal consistency of the scale, was calculated as 0.947. The test-retest reliability was found to be high (intraclass correlation coefficient=0.928). This study suggests that the Turkish version of PFS is valid and reliable. PFS is suitable for use by researchers and healthcare professionals to assess fatigue in Turkish-speaking patients with PD. © 2018 Wolters Kluwer Health, Inc. All rights reserved.Item Development of liquid crystal biosensor for the detection of amyloid beta-42 levels associated with Alzheimer's disease(Elsevier B.V., 2021) Kemiklioglu E.; Tuncgovde E.B.; Ozsarlak-Sozer G.This study represents the development of a biosensor which is based on the liquid crystal (LC) orientation as a function of the peptide concentration to detect an amyloid-beta-42 (Aβ42) antibody–antigen binding events. The Aβ42 peptide binds to the Aβ42 antibody forming an immunocomplex which is immobilized on the Dimethyloctadecyl[3-(trimethoxysilyl)propyl] ammonium chloride (DMOAP) coated surface. The disturbed orientation of LCs as a result of the binding of the formed immunocomplex was observed using the polarized optical microscope (POM) as a function of decreasing Aβ42 peptide concentration from 1000 to 1 pg/ml. The concentration, as low as 1 pg/ml of Aβ42 peptide was able to be successfully detected in our system. Apolipoprotein E4 (ApoE4), that specifically bound to the Aβ42 peptide, was added into the system and a remarkable change in reflection spectra of samples was observed with increasing Aβ42 peptide concentration. The concentration of ApoE4 protein was detected in the range of 0.1–30 nM by this system due to the interaction between the two proteins. © 2021 The Society for Biotechnology, Japan