Prediction and evaluation of purine-binding peptides using integrated molecular descriptors and docking analysis

Area of Science:

• Food Science
• Biochemistry
• Molecular Interactions

Background:

• Peptides and purines interact in food, affecting purine properties and bioavailability.
• The structural basis of these peptide-purine interactions is not well understood.

Purpose of the Study:

• To investigate the molecular mechanisms of peptide-purine binding.
• To develop a screening approach for identifying peptides with high purine-binding affinity.

Main Methods:

• Utilized molecular docking and descriptor analysis to screen peptide-purine interactions.
• Employed fluorescence spectroscopy to validate computational findings.
• Focused on hypoxanthine as a key dietary purine in processed meats.

Main Results:

• Strong peptide binders typically have fewer cyclic structures and aromatic rings, but more electron-donor groups (N, O atoms).
• Hydrogen bonding and hydrophobic interactions stabilize peptide-purine complexes.
• The tetrapeptide WDQW showed stable binding with hypoxanthine, validated by experiments.

Conclusions:

• Identified key molecular features of peptides that enhance purine binding.
• Established a screening platform for purine-binding peptides.
• Findings can inform strategies to modulate purine bioavailability in food systems.