Glycation Effects on Protein Structure and Allergenicity

Glycation is a non-enzymatic process in which reducing sugars react with amino groups of proteins, leading to a cascade of chemical modifications collectively known as the Maillard reaction. Early glycation adducts can rearrange into advanced glycation end-products (AGEs), which introduce covalent cross-links, alter surface charge and hydrophobicity, and promote protein aggregation. These structural perturbations can mask or expose conformational epitopes, modulate digestibility and influence recognition by immune receptors. In food systems, thermal processing in the presence of sugars accentuates glycation and AGE formation, reshaping allergenic potential. In a biomedical context, glycation-induced AGEs interact with cell-surface receptors to trigger inflammatory pathways. By altering tertiary and quaternary structures, glycation can both diminish antibody binding to known epitopes and generate neo-epitopes with enhanced immunogenicity. Understanding these dual impacts is critical for food formulation, allergy mitigation and the management of AGE-related pathologies.

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Glycation Effects on Protein Structure and Allergenicity publication trend

The graph below shows the total number of articles in glycation effects on protein structure and allergenicity across all publications each year (not limited to Nature Index journals).

Technical terms

Maillard reaction: A complex series of non-enzymatic reactions between reducing sugars and amino groups on proteins, leading to browning and formation of advanced glycation end-products.

Advanced glycation end-products (AGEs): Stable, often cross-linked molecules formed from the further rearrangement and oxidation of initial glycation adducts, implicated in altered protein function and inflammation.

Lactosylation: A form of glycation in which lactose covalently attaches to specific amino acid residues, used to modulate protein immunogenicity.

Epitope: The precise molecular region on an antigen recognised by an antibody or immune receptor; changes in epitope presentation affect allergenic potential.

RAGE: Receptor for advanced glycation end-products, a cell-surface receptor that binds AGEs and triggers pro-inflammatory signalling pathways.

References

1. The decrease in the IgG-binding capacity of intensively dry heated whey proteins is associated with intense Maillard reaction, structural changes of the proteins and formation of RAGE-ligands. Food & Function (2016).
2. Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition. Nutrients (2019).
3. Limited Lactosylation of Beta-Lactoglobulin from Cow’s Milk Exerts Strong Influence on Antigenicity and Degranulation of Mast Cells. Nutrients (2021).