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Journals / Türk Biyokimya Dergisi / 2019 / Cilt: 44 - Sayı: 4

Investigation of relaxation times in 5-fluorouracil and human serum albumin mixtures

5-Fluorouracil ve İnsan Serum Albümin Karışımlarında Rölaksasyon Zamanlarının İncelenmesi

Bilgin ZENGİN
Ali YILMAZ
Sibel KORUNUR
Pages
524–529
Publication Date
2022-11-05
DOI
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

NMR isrecognized as a valuable method to determine the structure of proteins-ligand and protein-drug complexes.Objective – Aim of the study: In this study, protein druginteractions were investigated using 5-Fluorouracil anticancer drug and human serum albumin protein.Materials and methods: In this context 400 MHz NMRspectrometry was used and NMR relaxation rates indrug-albumin complex were investigated with respect toincrease albumin concentration and increase in 5-Fluorouracil (5-FU)-albumin solution temperature.Results: The results of this study indicated that 5-FU hada weak association with albumin, and it easily dissociatedfrom the protein to which it was attached.Conclusion: The obtained results also gave us usefulinformation about molecular dynamics of drug-albumininteractions.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Background: Human serum albumin (HSA) is oftenselected as a subject of any study because albumin is themost abundant protein in human blood plasma.
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Key Findings & Data:Background: Human serum albumin (HSA) is oftenselected as a subject of any study because albumin is themost abundant protein in human blood plasma.
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Conclusion & Impact:NMR isrecognized as a valuable method to determine the structure of proteins-ligand and protein-drug complexes.Objective – Aim of the study: In this study, protein druginteractions were investigated using 5-Fluorouracil anticancer drug and human serum albumin protein.Materials and methods: In this context 400 MHz NMRspectrometry was used and NMR relaxation rates indrug-albumin complex were investigated with respect toincrease albumin concentration and increase in 5-Fluorouracil (5-FU)-albumin solution temperature.Results: The results of this study indicated that 5-FU hada weak association with albumin, and it easily dissociatedfrom the protein to which it was attached.Conclusion: The obtained results also gave us usefulinformation about molecular dynamics of drug-albumininteractions.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Abstract

Background: Human serum albumin (HSA) is oftenselected as a subject of any study because albumin is themost abundant protein in human blood plasma. NMR isrecognized as a valuable method to determine the structure of proteins-ligand and protein-drug complexes.Objective – Aim of the study: In this study, protein druginteractions were investigated using 5-Fluorouracil anticancer drug and human serum albumin protein.Materials and methods: In this context 400 MHz NMRspectrometry was used and NMR relaxation rates indrug-albumin complex were investigated with respect toincrease albumin concentration and increase in 5-Fluorouracil (5-FU)-albumin solution temperature.Results: The results of this study indicated that 5-FU hada weak association with albumin, and it easily dissociatedfrom the protein to which it was attached.Conclusion: The obtained results also gave us usefulinformation about molecular dynamics of drug-albumininteractions.

Özet

Geçmiş: İnsan serum albümini (HSA) sıklıkla herhangi bir çalışmanın konusu olarak seçilir çünkü albümin, insan kan plazmasında en bol bulunan proteindir. NMR, protein-ligand ve protein-ilaç komplekslerinin yapısını belirlemek için değerli bir yöntem olarak kabul edilmektedir. Amaç – Aim of the study: Bu çalışmada, 5-Fluorourasil anti-kanser ilacı ve insan serum albümin proteini kullanılarak protein ilaç etkileşimleri araştırılmıştır. Araç ve Yöntemler: Bu bağlamda, 400 MHz NMR spektrometresi kullanılmış ve ilaç-albümin kompleksi içindeki NMR rölaksasyon (gevşeme) oranları, albümin konsantrasyonunun arttırılması ve 5-Flüoroürasil (5-FU)-albümin çözelti sıcaklığındaki artış açısından incelenmiştir. Bulgular: Bu çalışmanın sonuçları, 5-FU’nun albümin ile zayıf bir ilişkisinin olduğunu ve ekli olduğu proteinden kolayca ayrıldığını göstermiştir. Sonuç: Elde edilen sonuçlar bize ilaç-albümin etkileşimlerinin moleküler dinamikleri hakkında da faydalı bilgiler vermiştir.

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Cite This Article

ZENGİN, B., YILMAZ, A., KORUNUR, S. (2022). Investigation of relaxation times in 5-fluorouracil and human serum albumin mixtures. Türk Biyokimya Dergisi, Cilt: 44 - Sayı: 4, 524–529. https://ajindex.com/articles/620842

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References (14)

  1. Peters Jr T. Serum albumin. Adv Protein Chem 1985;37:161–245
  2. He XM, Carter DC. Atomic structure and chemistry of human serum albumin. Nature 1992;358:209–15
  3. Ishida S, Kinoshita M, Sakiya Y, Taira Z, Ichikawa T. Glycyrrhizin binding site on human serum albumin. Chem Pharm Bull 1992;40:275–8
  4. Rahman MH, Yamasaki M, Shin YH, Lin CC, Otagiri M. Characterization of high affinity binding sites of non-steroidal anti-inflammatory drugs with respect to site-specific probes on human serum albumin. Biol Pharm Bull 1993;16:1169–74
  5. Ghuman J, Zunszain PA, Petitpas I, Bhattacharya AA, Otagiri M, Curry S. Structural basis of the drug-binding specificity of human serum albumin. J Mol Biol 2005;353:38–52
  6. Sun P, Hoops A, Hartwick RA. Enchanced albumin protein separations and protein-drug binding constant measurements using anti-inflammatory drugs as run buffer additives in affinity capillary electrophoresis. J Chromatogr B Biomed Appl 1994;661:335–40
  7. Ascoli G, Bertucci C, Salvadori P. Stereospecific and competitive binding of drugs to human serum albumin: a difference circular dichroism approach. J Pharm Sci 1995;84:737–41
  8. Aubry AF, Markoglou N, Mcgann A. Comparison of drug binding interactions on human, rat and rabbit serum albumin using highperformance displacement chromatography. Comp Biochem Physiol C Pharmacol Toxicol Endocrinol 1995;112:257–66
  9. Epps DE, Raub TJ, Kezdy FJ. A general, wide-range spectrofluorometric method for measuring the site-specific affinities of drugs toward human serum albumin. Anal Biochem 1995;227:342–50
  10. Castillo M, Smith PC. Disposition and reactivity of ibuprofen and ibufenac acyl glucuronides in vivo in the rhesus monkey and in vitro with human serum albumin. Drug Metab Dispos 1995;23:566–72
  11. Blondeau JP, Robel P. Determination of protein-ligand binding constants at equilibrium in biological samples. Eur J Biochem 1975;55:375–84
  12. Hage DS, Noctor TA, Wainer IW. Characterization of the protein binding of chiral drugs by high-performance affinity chromatography interactions of R- and S-ibuprofen with human serum albumin. J Chromatogr A 1995;693:23–32
  13. Hashimoto S, Yabusaki T, Takeuchi H, Harada I. Structure and ligand-binding modes of human serum albumin studied by UV resonance raman spectroscopy. Biospectroscopy 1995;1:375–85
  14. Cheruvallath VK, Riley CM, Narayanan SR, Lindenbaum S, Perrin JH. The effect of octanoic acid on the binding of the enantiomers of ibuprofen and naproxen to human serum