Calcium binding to herring egg phosphopeptides: Binding characteristics, conformational structure and intermolecular...

Area of Science:

• Biochemistry
• Food Science
• Materials Science

Background:

• Phosphorylation can improve protein functionality.
• Herring egg peptides have potential phosphorylation sites for functional enhancement.

Purpose of the Study:

• To investigate the impact of phosphorylation on the calcium-binding ability of herring egg peptides.
• To analyze the conformational structure and intermolecular forces within herring egg phosphopeptides (HEPPs)-calcium complexes.

Main Methods:

• Preparation of phosphorylated herring egg peptides (HEPPs).
• Assessment of calcium-binding activity in HEPPs versus non-phosphorylated peptides.
• Analysis of the conformational structure and intermolecular forces of HEPPs-calcium complexes using techniques like spectroscopy and microscopy.

Main Results:

• HEPPs exhibited significantly enhanced calcium-binding activity compared to non-phosphorylated peptides.
• Calcium binding induced the formation of β-sheet structures and conformational folding in HEPPs.
• HEPPs-calcium complexes self-assembled into spherical nanoparticles.

Conclusions:

• Phosphorylation effectively improves the calcium-binding capacity of herring egg peptides.
• The interaction between calcium ions and phosphate groups is key to enhanced binding.
• HEPPs-calcium nanoparticles are stabilized by hydrophobic interactions, hydrogen bonds, and electrostatic forces, indicating potential applications in biomaterials or nutraceuticals.