The interaction of pyridoxine (Vita

The interaction of pyridoxine (Vitamin B6) with bovine serum albumin (BSA) is investigated under
pseudo-physiological conditions by UV–Vis, fluorescence and FTIR spectroscopy. The intrinsic fluorescence
of BSA was quenched by VB6, which was rationalized in terms of the static quenching mechanism.
According to fluorescence quenching calculations, the bimolecular quenching constant (kq), dynamic
quenching (KSV) and static quenching (KLB) at 310 K were obtained. The efficiency of energy transfer
and the distance between the donor (BSA) and the acceptor (VB6) were calculated by Foster’s nonradiative
energy transfer theory and were equal to 41.1% and 2.11 nm.
The collected UV–Vis and fluorescence spectra were combined into a row-and column-wise augmented
matrix and resolved by multivariate curve resolution-alternating least squares (MCR-ALS). MCR-ALS
helped to estimate the stoichiometry of interactions, concentration profiles and pure spectra for three
species (BSA, VB6 and VB6-BSA complex) existed in the interaction procedure. Based on the MCR-ALS
results, using mass balance equations, a model was developed and binding constant of complex was calculated
using non-linear least squares curve fitting. FT-IR spectra showed that the conformation of proteins
was altered in presence of VB6. Finally, the combined docking and molecular dynamics (MD)
simulations were used to estimate the binding affinity of VB6 to BSA. Five-nanosecond MD simulations
were performed on bovine serum albumin (BSA) to study the conformational features of its ligand binding
site. From MD results, eleven BSA snapshots were extracted, at every 0.5 ns, to explore the binding
affinity (GOLD score) of VB6 using a docking procedure. MD simulations indicated that there is a considerable
flexibility in the structure of protein that affected ligand recognition. Structural analyses and docking
simulations indicated that VB6 binds to site I and GOLD score values depend on the conformations of
both BSA and ligand. Molecular modeling results showed that VB6–BSA complex formed not only on the
basis of electrostatic forces, but also on the basis of p–p staking and hydrogen bond. There was an excellent
agreement between the experimental and computational results. The results presented in this paper,
will offer a reference for detailed and systematic studies on the biological effects and action mechanism
of small molecules with proteins.

ผลลัพธ์ (อังกฤษ) 2:

The Interaction of pyridoxine (Vitamin B6) with bovine serum albumin (BSA) is investigated under
physiological conditions by UV-Vis-Pseudo, FTIR and fluorescence spectroscopy. The intrinsic fluorescence
of BSA was quenched by VB6, which was rationalized in terms of the static quenching mechanism.
According to fluorescence quenching calculations, the bimolecular quenching Constant (KQ), Dynamic
quenching (KSV) and static quenching (KLB) at 310 K were. obtained. The efficiency of Energy Transfer
and the Distance between the donor (BSA) and the acceptor (VB6) were calculated by Foster's Nonradiative
Energy Transfer Theory and were Equal to 41.1% and 11.02 NM.
The Collected UV-Vis and fluorescence Spectra were combined Into a. Row-and-column Wise Augmented
Matrix and Resolved by Alternating Least-squares multivariate Curve resolution (MCR-ALS). MCR-ALS
helped to Estimate the stoichiometry of interactions, and concentration profiles for Pure Spectra Three
species (BSA, VB6 and VB6-BSA Complex) existed in the Interaction procedure. MCR-ALS based on the
results, using mass balance equations, a Model was developed and binding of Constant Complex was calculated
using non-linear Curve fitting Least squares. FT-IR Spectra Showed that the conformation of Proteins
Altered was in Presence of VB6. Finally, the combined molecular and Docking Dynamics (MD)
simulations were used to Estimate the binding affinity of VB6 to BSA. Five-nanosecond MD simulations
were performed on bovine serum albumin (BSA) to Study the conformational features of ITS ligand binding
Site. Results from MD, BSA Eleven snapshots were extracted, at every 0.5 ns, to explore the binding
affinity (GOLD Score) of VB6 using a Docking procedure. MD simulations indicated that there is a considerable
flexibility in the structure of that protein ligand AFFECTED Recognition. Docking structural analyzes and
simulations indicated that binds to VB6 Site I and GOLD Score values ​​Depend on the conformations of
both BSA and ligand. Modeling results Showed that VB6 molecular-BSA Complex formed not only on the
basis of electrostatic Forces, but also on the basis of P-P Bond staking and hydrogen. There was an Excellent
Agreement between the Computational and experimental results. Presented the results in this Paper,
Will Offer Reference for a detailed and systematic Biological Studies on the effects and mechanism Action
of Small molecules with Proteins.