Author:
Benamara Hacen,Lanez Touhami,Lanez Elhafnaoui
Abstract
The binding affinity of 2-ferrocenylbenzonitrile (2FBN) and 4-ferrocenylbenzonitrile (4FBN) with bovine serum albumin (BSA) has been investigated by cyclic voltammetry, absorption spectroscopy and molecular modelling techniques. The results indicated that both of the two derivatives could bind to BSA and cause conformational changes with the order 2FBN > 4FBN. The voltammetric behavior of 2FBN and 4FBN before and after the addition of the BSA suggests that the redox process is kinetically controlled by the diffusion step, and demonstrated that the diffusion coefficients of the 2FBN-BSA and 4-FBN-BSA adducts are lower than that of the free compounds. Furthermore, molecular docking suggested that the binding mode of the two compounds to BSA is of hydrophobic and hydrogen bond interactions, moreover the ligand 2FBN additionally show a π-cation interaction.
Publisher
International Association of Physical Chemists (IAPC)
Subject
Electrochemistry,Materials Chemistry,Colloid and Surface Chemistry,Chemical Engineering (miscellaneous)
Cited by
3 articles.
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