Virtual Screening of Soybean Protein Isolate-Binding Phytochemicals and Interaction Characterization

Area of Science:

• Food Science
• Biochemistry
• Computational Chemistry

Background:

• Soybean protein isolate (SPI) interactions with small molecules are gaining interest.
• Limited large-scale studies compare different phytochemical compounds for SPI binding.

Purpose of the Study:

• To identify potential phytochemical binders for soybean protein isolate (SPI) using high-throughput virtual screening.
• To characterize the molecular interactions between SPI and selected phytochemicals.

Main Methods:

• High-throughput virtual screening of 1130 compounds against SPI.
• Validation using fluorescence quenching assays to determine binding constants (Ka).
• Molecular dynamics (MD) simulations to analyze interface interactions and binding forces.

Main Results:

• Isoginkgetin exhibited the highest apparent binding constant (Ka) at (0.060 ± 0.020) × 10^6 L·mol^-1.
• MD simulations identified hydrogen bonding with residues E172, H173, G202, and V204 as crucial for isoginkgetin binding to SPI.
• Van der Waals forces were determined to be the primary driving force for isoginkgetin-SPI complex formation.

Conclusions:

• Isoginkgetin is identified as a novel binder for soybean protein isolate (SPI).
• Detailed molecular insights into SPI-phytochemical interactions were revealed.
• Findings have significant implications for developing SPI-phytochemical complexes in food applications.