Hen egg-white lysozyme aggregation interface

Hen egg-white lysozyme is a small, stable enzyme (129 amino acids) that hydrolyzes β(1→4) glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in bacterial cell walls, thereby conferring antibacterial activity. The enzyme is highly abundant in bird egg whites and secretions like tears and saliva, serving an important defensive role in innate immunity. The aggregation interface refers to structural regions of lysozyme that interact during protein aggregation under destabilizing conditions—such as elevated temperature or altered pH—leading to the formation of amyloid-like fibrils. Aggregation studies are primarily biophysical and relate to understanding protein misfolding, not to drug targeting. If your intent is to catalog molecular targets for drug development or clinical applications, revert to "Hen egg-white lysozyme" (HEWL) rather than the aggregation interface, as only the enzyme has established classification, function, and aliases. The aggregation interface is a laboratory research concept and not a canonical target.

Other names

LysozymeMuramidaseHEWL

Not applicable for aggregation interface. Lysozyme enzyme itself cleaves β(1→4) glycosidic bonds in peptidoglycans