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- MakaleAçık Erişim2019Scopus SJRQ4Investigation of relaxation times in 5-fluorouracil and human serum albumin mixtures
Korunur, Sibel; Zengin, Bilgin; Yilmaz, Ali
Background: Human serum albumin (HSA) is often selected as a subject of any study because albumin is the most abundant protein in human blood plasma. NMR is recognized as a valuable method to determine the structure of proteins-ligand and protein-drug complexes. Objective - Aim of the study: In this study, protein drug interactions were investigated using 5-Fluorouracil anticancer drug and human serum albumin protein. Materials and methods: In this context 400 MHz NMR spectrometry was used and NMR relaxation rates in drug-albumin complex were investigated with respect to increase albumin concentration and increase in 5-Fluoro-uracil (5-FU)-albumin solution temperature. Results: The results of this study indicated that 5-FU had a weak association with albumin, and it easily dissociated from the protein to which it was attached. Conclusion: The obtained results also gave us useful information about molecular dynamics of drug-albumin interactions.
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İncele - MakaleYalnız künye2018Scopus SJRQ4400 MHz NMR Study of Isotope Effects on Albumin in H2O/D2O Solutions
Korunur, S.; Zengin, B.; Yılmaz, A.
Abstract: Chemical shift measurements were performed for several percentages of H2O added to D2O, in several H2O/D2O mixtures without and with a single concentration of albumin, and also in a mixture of 0.1H2O/0.9D2O containing increasing concentrations of albumin. The chemical shifts of pure mixtures decreases with increasing fraction of pure water. This is closely related to isotope effects. The chemical shift corrected for isotope effects increases with percentage of H2O. The chemical shift obtained for the mixture of 0.1H2O/0.9D2O increases with increasing concentration of albumin. These increments are consistent with fast chemical exchange in H2O/D2O mixture. In conclusion, present study reveals the presence of isotope effect on albumin in H2O/D2O solutions, and demonstrates fast chemical exchange in D2O solutions with albumin in a different way.
AtıfScopus1WoS1OpenAlex1İncele - MakaleYalnız künye2017Scopus SJRQ3The examination of a variety of different ions added to the crown ether derivatives with high field NMR spectrometer
Aşkin, Muzaffer; Zengin, Bilgin; Korunur, Sibel; Kor, Harun; Köylü, M. Zafer
The current study involves the measurements of T1 relaxation time of complexes three different crown ethers (4-aminobenzo-15-Crown-5, 1-Aza-18-Crown-6, 1-Aza-15-Crown-5) and two different ions sodium perchlorate (NaClO4), lithium perchlorate (LiClO4) by a 400 MHz NMR spectrometer. The association constants (Ka) of the complexes were determined on the basis of the evaluation of these measurements using the Benesi-Hildebrand method that we have modified. These association constants were consistent with those obtained from 1H NMR titration technique. As a result, it can be speculated that binding constants could be measured using T1 relaxation time when chemical shifts are very small or cannot be observed.
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