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Investigation of the Interaction between Coumarins and Its Derivatives with Human Serum Albumin: STD-NMR, Fluorescence and Docking Molecular Studies

Author

Listed:
  • Fatima Pereira de Souza
  • Fernanda Paulin Benzatti
  • Ã caro P. Caruso
  • Thiago Salem Pançonato Teixeira
  • Fábio Rogério Moraes
  • Fernando Alves de Melo
  • Luiz Claudio Di Stasi
  • Marinônio Lopes Cornélio
  • Marcelo Andres Fossey

Abstract

In this paper, binding interaction of Coumarin, including 4-Methylesculetin, Esculetin and Esculin, with human serum albumin (HSA) was investigated by using STD-NMR, fluorescence spectroscopy and molecular docking method. STD-NMR investigations indicated that the binding affinity sequence for HSA-ligands interaction was: 4-Methyllesculetin >Esculetin>Coumarin>Esculinbeingin accordance with the fluorescence studies. The molecular docking resultssuggested that coumarins and its derivatives were binding to HSA at subdomain IIA, nearby the Trp214 residue, which are consistent with the results of fluorescence quenching results. Overall, the experimental and theoretical data corroborate with each other and they are complementary.

Suggested Citation

  • Fatima Pereira de Souza & Fernanda Paulin Benzatti & à caro P. Caruso & Thiago Salem Pançonato Teixeira & Fábio Rogério Moraes & Fernando Alves de Melo & Luiz Claudio Di Stasi & Marinônio Lopes Co, 2016. "Investigation of the Interaction between Coumarins and Its Derivatives with Human Serum Albumin: STD-NMR, Fluorescence and Docking Molecular Studies," International Journal of Sciences, Office ijSciences, vol. 5(02), pages 1-11, February.
    • Handle: RePEc:adm:journl:v:5:y:2016:i:2:p:1-11
    DOI: 10.18483/ijSci.777
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