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Noncovalent Interactions of Bovine Trypsin with Curcumin and Effect on Stability, Structure, and Function by Mina Rajabi; Sadegh Farhadian; Behzad Shareghi; Sanaz Asgharzadeh; Lida Momeni is a Materials Science article available to read on EtoBox.

What is Noncovalent Interactions of Bovine Trypsin with Curcumin and Effect on Stability, Structure, and Function about?

The structural studies of trypsin with curcumin in Tris-hydrochloride (Tris-HCl) buffer solution (pH 8.0) was explored by UV-vis spectroscopic and fluorescence quenching method, kinetic reaction, circular dichroism (CD), Thermal denaturation, molecular docking, and molecular dynamic simulation. The curcumin could decrease trypsin absorbance. It was showed that curcumin could quench the fluorescence of trypsin by static quenching mechanism. This is in agreement with UV-vis results and CD studies in which the α-helix becomes more, and β-sheet becomes less than trypsin without ligand. The binding constant, the number of binding sites and thermodynamic parameters (ΔH°, ΔS°, and ΔG°) at two temperatures were calculated. The hydrogen bond and Van der Waals interaction were found as the main forces, which is in congruence with docking results. The outcome of the kinetic reaction indicates an uncompetitive inhibition by curcumin on trypsin. Molecular Dynamic simulation and Thermal denaturation results demonstrate that curcumin makes trypsin unstable and more flexible.

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Author

Mina Rajabi; Sadegh Farhadian; Behzad Shareghi; Sanaz Asgharzadeh; Lida Momeni

Publisher

Elsevier BV

Published

2019

Language

EN

Field

Materials Science (Physical Sciences)