Patients with sickle cell disease have mutant haemoglobin proteins that form deadly long, stiff fibres inside red blood cells. A research team led by University of Warwick researcher Dr Matthew Turner, propose a mathematical model in the 28 March online issue of PRL to explain the persistent stability of these deadly fibres. The theory suggests that an inherent "twistiness" in the strands that make up the fibres could be the key to their durability and possibly to new treatments.
Red blood cells supply oxygen to the body using their cargo of haemoglobin, a protein that can capture and release oxygen. Haemoglobin molecules normally float freely in the cell, but sickle cell patients have a mutated, "sticky," form of haemoglobin that tends to clump together into long fibres. The stiff fibres form a scaffolding that distorts the cells into their namesake "sickle" shape, so they jam up trying to pass through small blood vessels. The traffic jams deprive vital organs of oxygen, so patients end up with anaemia, jaundice, major organ damage, and many other maladies.
A sickle haemoglobin fibre can be made up of anywhere from 14 to more than 400 individual strands of haemoglobin molecules linked into long chains. Matthew Turner, of the University of Warwick in the UK, wondered why these strands tend to clump together into long, stiff, fibres rather than compact crystals, which would be less harmful. "A scaffolding made of the rigid fibres is much worse than a couple little sugar-cube-like crystals floating around," Turner says. So he and his colleagues constructed a mathematical model.
Peter Dunn | alfa
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