This is a second part of the three-part article from a series of reviews on the abundance and roles of intrinsic
disorder in milk proteins. We continue to describe α-lactalbumin, a small globular Ca2+-binding protein, which besides
being one of the two components of lactose synthase that catalyzes the final step of the lactose biosynthesis in the lactating
mammary gland, possesses a multitude of other functions. In fact, recent studies indicated that some partially folded
forms of this protein possess noticeable bactericidal activity and other forms might be related to induction of the apoptosis
of tumor cells. In its anti-tumorigenic function, oligomeric α-lactalbumin serves as a founding member of a new family of
anticancer drugs termed liprotides (for lipids and partially denatured proteins), where an oligomeric molten globular protein
acts as an “oil container” or cargo for the delivery of oleic acid to the cell membranes.
Keywords: α-lactalbumin; intrinsic disorder, liprotide, molten globule, oleic acid binding, stability, structure.
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