2026-10-29T22:55:14Zhttps://munzur-rdlopen.rawdatalibrary.net/oai/requestoai:munzur-rdlopen.rawdatalibrary.net:munzur/36082026-10-28T15:39:32Zopenairedrivercom_munzur_1col_munzur_2com_munzur_8col_munzur_154com_munzur_11col_munzur_162Investigation of relaxation times in 5-fluorouracil and human serum albumin mixturesKorunur, SibelZengin, BilginYilmaz, Ali5-FluorouracilHuman serum albuminNMRRelaxation ratesTemperatureBackground: 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.De Gruyter2019Articlehttps://rdlopen.rawdatalibrary.net/r/munzur/3608https://doi.org/10.1515/tjb-2017-03630250-4685enTurkish Journal of Biochemistryinfo:eu-repo/semantics/openAccessinfo:eu-repo/semantics/articlehttps://munzur-rdlopen.rawdatalibrary.net/tr/items/munzur/3608