Molecular Recognition Patterns between Vitamin B12 and Proteins Explored through STD-NMR and In Silico Studies

Area of Science:

• Biochemistry
• Molecular Biology
• Structural Biology

Background:

• Ligand-receptor interactions are fundamental to biological processes.
• Saturation Transfer Difference-NMR (STD-NMR) provides atomic-resolution data on physiological interactions.
• Understanding nutrient-protein binding is crucial for biological action.

Purpose of the Study:

• To investigate molecular recognition patterns between cyanocobalamin (CNBL)/aqua cobalamin (OHBL) and various proteins.
• To determine and compare the binding affinities of different proteins for CNBL and OHBL.
• To validate experimental findings with theoretical computer simulations.

Main Methods:

• Saturation Transfer Difference-NMR (STD-NMR) spectroscopy was employed to study binding.
• Molecular docking simulations were used to complement experimental data.
• Binding affinities were assessed for plant and animal proteins, including myoglobin, casein, and gluten.

Main Results:

• Myoglobin demonstrated the highest binding affinity for cobalamins.
• Gluten exhibited the lowest binding affinity among the tested proteins.
• Casein showed moderate binding affinity for both CNBL and OHBL, higher than plant proteins.

Conclusions:

• STD-NMR and molecular docking successfully elucidated cobalamin-protein recognition modes.
• The study provides a quantitative understanding of cyanocobalamin binding affinities.
• This research highlights the utility of NMR technology in linking nutrient properties to biological functions.