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Interaction of major saffron constituent safranal with trypsin: An experimental and computational investigation.
Ali, Mohd Sajid; Teixeira, Luís M C; Ramos, Maria J; Fernandes, Pedro A; Al-Lohedan, Hamad A.
Afiliación
  • Ali MS; Department of Chemistry, College of Science, King Saud University, P.O. Box-2455, Riyadh 11451, Saudi Arabia. Electronic address: msali@ksu.edu.sa.
  • Teixeira LMC; LAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências,Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.
  • Ramos MJ; LAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências,Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.
  • Fernandes PA; LAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências,Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.
  • Al-Lohedan HA; Department of Chemistry, College of Science, King Saud University, P.O. Box-2455, Riyadh 11451, Saudi Arabia.
Int J Biol Macromol ; 274(Pt 2): 133231, 2024 Aug.
Article en En | MEDLINE | ID: mdl-38897495
ABSTRACT
Trypsin is a serine protease, an important digestive enzyme that digests the proteins in the small intestine. In the present study, we have investigated the interaction of safranal, a major saffron metabolite, with trypsin using spectroscopic and molecular docking analyses. Fluorescence emission spectra of trypsin were largely affected by the inner filter effect from safranal; that's why these were corrected using the standard procedure. The corrected fluorescence spectra have shown that the safranal quenched the intrinsic fluorescence of trypsin with a blue shift in the wavelength of emission maximum, which revealed that the microenvironment of the fluorophore became more hydrophobic. There was approximately 1 1 fair binding between them, which increased with a rise in temperature. The interaction was favored, principally, by hydrophobic forces, and there was an efficient energy transfer from the fluorophore to the safranal. Synchronous fluorescence spectra suggested that the tryptophan residues were the major ones taking part in the fluorescence quenching of trypsin. Safranal also influenced the secondary structure of trypsin and caused partial unfolding. Molecular Docking and the Molecular Dynamics simulation of the free and complexed trypsin was also carried out. Safranal formed a stable, non-covalent complex within the S2'-S5' subsite. Moreover, two nearby tyrosine residues (Tyr39 and Tyr151) stabilized safranal through π-π interactions. Additionally, the presence of safranal led to changes in the protein flexibility and compactness, which could indicate changes in the surrounding of tryptophan residues, impacting their fluorescence. Furthermore, a loss in compactness is in line with the partial unfolding observed experimentally. Thus, both experimental and computational studies were in good agreement with each other.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Terpenos / Tripsina / Crocus / Ciclohexenos / Simulación de Dinámica Molecular / Simulación del Acoplamiento Molecular Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Terpenos / Tripsina / Crocus / Ciclohexenos / Simulación de Dinámica Molecular / Simulación del Acoplamiento Molecular Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos