pH-Dependent Reversible Self-Assembly of β-Lactoglobulin-Derived Reducing Peptides

Area of Science:

• Biomaterials Science
• Protein Chemistry
• Nanotechnology

Background:

• Peptide-based self-assembled nanostructures are promising for nutrient delivery and interface engineering.
• Beta-lactoglobulin (β-Lg) is a well-studied milk protein with potential for peptide derivation.

Purpose of the Study:

• To screen β-Lg derived peptides for pH-dependent self-assembly.
• To investigate the fibrilization mechanisms and properties of identified peptides.
• To explore the potential applications of these peptide nanostructures.

Main Methods:

• Screening of eight β-Lg derived peptides.
• pH-cycling experiments to induce reversible fibrilization.
• Characterization of fibril structure using cross-β sheet analysis.
• Assessment of antioxidant capacity and stability under simulated digestion.

Main Results:

• Two peptides, EV-10 and VR-7, showed pH-dependent reversible fibrilization.
• EV-10 formed fibrils at pH 2.0, VR-7 at pH 7.0, with both exhibiting reversible transitions.
• Fibril formation was influenced by N- and C-terminal charges, forming antiparallel cross-β structures.
• EV-10 fibrils demonstrated sustained Fe3+ reduction capacity and stability in simulated gastric conditions.

Conclusions:

• β-Lg derived peptides can form smart pH-responsive self-assembled nanostructures.
• These nanostructures offer potential for controlled nutrient delivery and long-term antioxidant protection.
• Understanding fibrilization mechanisms aids in designing advanced biomaterials for various applications.