Atomistic Modeling of Peptide Aggregation and β-Sheet Structuring in Corn Zein for Viscoelasticity

Area of Science:

• Biochemistry
• Materials Science
• Food Science

Background:

• Plant-based proteins lack defined structure-function relationships for meat-like texture.
• Engineering viscoelasticity in plant proteins is crucial for cohesiveness and mouthfeel.
• Intermolecular β-sheet structures are known to improve protein viscoelastic properties.

Purpose of the Study:

• Investigate peptide segments in corn α-zein variants for stable aggregates and β-sheet structures.
• Determine factors influencing β-sheet structuring and stability in zein peptides.
• Provide insights into enhancing zein viscoelasticity for plant-based meat analogues.

Main Methods:

• Molecular simulations of dimer and eight-peptide β-sheet oligomer systems.
• Analysis of peptide stability, orientation, and hydrophobic residue influence.
• Quantification of β-sheet conformation based on dimer hydrogen-bonding density.

Main Results:

• Zein peptide stability depends on initial orientation and hydrophobic residues.
• Proline-free peptide sequences exhibit higher β-sheet structuring.
• A dimer hydrogen-bonding density exceeding 22% correlates with increased β-sheet conformation.

Conclusions:

• Identified key sequence features (e.g., proline absence, hydrogen-bonding density) for enhanced β-sheet structuring in zein peptides.
• Demonstrated the potential of specific zein peptide segments to form stable aggregates and β-sheet structures.
• Contributed to understanding zein viscoelasticity for improved plant-based meat analogue development.