1. Investigation of relaxation times in 5-fluorouracil and human serum albumin mixtures.
- Author
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Korunur, Sibel, Zengin, Bilgin, and Yilmaz, Ali
- Subjects
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BLOOD proteins , *BLOOD plasma , *MOLECULAR dynamics , *PROTEIN drugs , *DRUG interactions , *SERUM albumin , *ALBUMINS - Abstract
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 anti-cancer 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-Fluorouracil (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. [ABSTRACT FROM AUTHOR]
- Published
- 2019
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