It has long been known that proteins change their conformation upon adsorption to emulsion
oil/water interfaces. However, it is only recently that details of the specifics of these structural …

α-Lactalbumin (α-LA) is a small (Mr 14,200), acidic (pI 4–5), Ca2+-binding protein. α-LA is a
regulatory component of lactose synthase enzyme system functioning in the lactating …

A complex formed by human α-lactalbumin (α-LA) and oleic acid (OA), named HAMLET, has
been shown to have an apoptotic activity leading to the selective death of tumor cells. In …

We show that all four classes of surfactants (anionic, cationic, non-ionic, and zwitterionic)
denature α-lactalbumin (αLA), making αLA an excellent model system to compare their …

The conformation and structural dimensions of α-lactalbumin (α-La) both in solution and
adsorbed at oil–water interfaces of emulsions were investigated using synchrotron radiation …

Protein–surfactant interaction is widely studied to understand stability and structural
changes in proteins. In this Article, we have investigated SDS-induced unfolding of RNase A …

The adsorption of eight different proteins (α-lactalbumin (types I and III), bovine serum
albumin, hemoglobin, myoglobin, cytochrome c, α-casein, and lysozyme) onto a model …

In order to highlight the role of hydrophobic interactions in the molten globule (MG) state of
globular protein modulated by surfactants, the interactions of bovine α-lactalbumin (α-LA) …

HAMLET (human alpha-lactalbumin made lethal to tumor cells) is a tumoricidal complex
consisting of partially unfolded protein and fatty acid and was first identified in casein …

The ability of antimicrobial peptides to efficiently kill their bacterial targets depends on the
efficiency of their binding to the microbial membrane. In the case of enterocins, there is a …