Lactoferrin Research Paper

Lactoferrin properties derive from the structural characteristics and its main function of iron uptake. Indeed, this glycoprotein actively participates in the regulation of the level of free iron in the body fluids. Under aerobic conditions unbounded iron ions catalyze redox transformations resulting in formation of toxic free radicals. These radicals are highly reactive, they attack the membranes, proteins, nucleic acids and many other cell components [17]. Thus, through the complexation of ferric ions, lactoferrin prevents the undesirable formation of free radicals and preserves iron ions in a bio-available and non-toxic form. It should be noted that, unsaturated form of lactoferrin is known for the bacteriorastic effect that possesses. This biochemical property derives from its primary function of iron sequestering thus depriving bacteria of iron from its nutrient medium [18]. Lactoferrin is involved in a considerable amount of many other physiological functions including anti-inflammatory [19], immunomodulatory [20] and anticarcinogenic [21,22] which make this protein even more valuable.
The experimental studies have shown that the substrate of lactoferrin changes the conformation in the course of the reaction, thus the iron-loaded form has a closed conformation whilst the iron-free form has an open conformation. The process is reversible and pH dependent, N-lobe releases iron at pH 5.0 whilst C-lobe retains iron till pH 3.0 [14]. These subtle differences in the properties of N- and C- protein lobes determine the conformation and functionality of the protein. In this sense three lactoferrin conformations are distinguished: the iron-free open form of lactoferrin (apolactoferrin), the monoferric form (N-lobe open and C-lobe closed conformation) and the iron loaded closed form (diferric lactoferrin, also known as