(Photo by ©Walt Disney Studios Motion Pictures)Īt their big Disney+ event in December of 2020, Disney announced two Disney+ series that were essentially Iron Man spinoffs: Ironheart (which is still set to be a show in 2023) and Armor Wars, based on the classic 1980s comic book storyline and focused on Don Cheadle’s War Machine character. 2 Lactoferricin has been found to prevent cellular growth by inhibiting the function of proteins involved in cellular reproduction.This WEEK’S TOP STORY MARVEL’S ARMOR WARS NOW BEING DEVLOPED AS A FILM 2 Recent research has taken particular interest in using lactoferrin as an oral cancer treatment, because when it is digested in the stomach, it is broken down to the peptide lactoferricin and absorbed into the bloodstream. 2 Additionally, this cationic region can bind to DNA, and thus serves as a defense against viruses by binding to viral DNA and preventing its spread through the body. 2 This binding feature allows lactoferrin to more directly attack bacteria because lipopolysaccharides and glycosaminoglycans are commonly found in the cell membrane of bacteria, and lactoferrin has been found to bind to the surfaces of bacteria and prevent iron uptake. 2 This basic region has been found to bind to lipopolysaccharides and glycosaminoglycans. The overall structure includes a unique cationic region on its N-terminal (See figure 3). In addition to its antibacterial defenses, lactoferrin performs other functions in the body. All transferrin proteins bind with high affinity to iron (III) ions, but lactoferrin has the highest binding affinity (K D ~ 10 -20 M compared with K D ~ 10 -9 M for transferrin). 4 The ability for lactoferrin to retain iron in a pH far below the biological level of 7.4 makes lactoferrin a more effective tool in the war over iron than transferrin, but less effective as an iron source for the body itself.įigure 2: Comparison of the structures of three iron chelating proteins in the transferrin family: Lactoferrin, transferrin, and ovotransferrin. 4 A pH of this acidity can be found in the body in places such as inflammation sites, cellular vesicles, or the stomach. 3 On the other hand, lactoferrin binds to iron with a much higher affinity, and the ion is not known to be released until pH drops to around 2-3. Transferrin has a lower binding affinity to iron than lactoferrin does, and a slight dip below biological pH can trigger the protein to release its ion. 2 Transferrin, while in some cases able to prevent bacterial infection, is used more efficiently as an iron transport protein. 2 Lactoferrin is a member of the transferrin family, a group of proteins that bind specifically to iron and perform various functions in the body (see figure 2). Left: human protein, lactoferrin.Įnter to the scene lactoferrin, a iron-chelating protein that has an extremely high binding affinity for iron (III). Faecalis siderophore, ferric hydroxamate. 1 As a result of this mutual need, iron wars break out between bacteria and the human body, and each side has used scientific methods to more efficiently acquire this resource.įigure 1: Cartoon depicting the “iron wars” between human and bacterial iron-sequestering proteins. 1 However, humans aren’t the only organisms that need this ion as a nutrient source bacterial species depend on ions like iron to survive. While largely known for its rusting abilities, iron is also the catalyst for numerous metabolic processes, a binding agent in molecules like hemoglobin, and is even speculated to be a contributing ion to the early formation of macromolecules that eventually led to life forms. Wars can be started over metals like gold or silver, but the human body wages an internal war against pathogens on a daily basis over a seemingly insignificant metal: iron (see figure 1).
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