HAMLET (protein complex)

In a 1995 study, it was discovered by Swedish scientist Anders Håkansson (Anders Hakansson) [2] that multimeric alpha-lactalbumin (MAL), a compound isolated from a fraction of human milk called casein, induced what appeared to be apoptosis in human lung carcinoma cells, pneumococcus bacteria, and other pathogens, while leaving healthy, differentiated cells unaffected.

[3] Endogenous human alpha-lactalbumin is complexed with a calcium ion and serves as a cofactor in lactose synthesis, but has no tumoricidal properties.

Furthermore, in vitro studies have shown that HAMLET is capable of binding the catalytic 20S subunit of the proteasome and disabling its enzymatic activity, an effect that has never before been demonstrated for any protein.

[10] HAMLET cells showed the physiological characteristics of macroautophagy, a process in which cellular components are sequestered in double membrane-bound vesicles that fuse with lysosomes for degradation.

Specifically, HAMLET can make MRSA bacteria sensitive against methicillin, vancomycin, gentamicin and erythromycin[12] Research is being conducted to determine if this could be a possible treatment for cancer.

[1] The first human trial of the therapy was on benign skin growths known as warts and showed positive outcomes without any side effects.

[1] It is being studied in carcinomas of the lung, throat, kidney, colon, bladder, prostate, and ovaries, as well as melanomas, glioblastomas, and leukemias.