A folding variant of human α-lactalbumin that may form in acidic environments such as the stomach, called HAMLET, probably induces apoptosis in tumor and immature cells.

[10] When formed into a complex with Gal-T1, a galactosyltransferase, α-lactalbumin, enhances the enzyme's affinity for glucose by about 1000 times, and inhibits the ability to polymerise multiple galactose units.

[11] One of the main structural differences with beta-lactoglobulin is that it does not have any free thiol group that can serve as the starting-point for a covalent aggregation reaction.

[12] These two proteins share much of their physical structure but contain less than half of the same amino acid sequence and therefore vary in function drastically.

[11] So, the expected evolutionary history is that gene duplication of the c-lysozyme was followed by mutation, resulting in the loss of lysozyme catalytic activity in α-lactalbumin.

This protein is a strong source of branched amino acids, cysteine, and tryptophan residues, each with correlated health benefits.

The protein also increases the plasma concentration for other large neutral amino acids (LNAAs) which help balance hormones.

[15][16] Cancer: There has been extensive research on apoptotic effects that α-lactalbumin potentially has when it forms a complex with oleic acid called HAMLET (Human alpha-lactalbumin made lethal to tumor cells).

This HAMLET complex disrupts the structure of the membrane when bound, promoting cell death to protect the integrity of the organism.