Researchers Say Deadly Twist Key To Sickle Cell Disease

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.

Bloodworm shows new use for copper

The lowly and somewhat gruesome bloodworm may have a few lessons to teach material scientists.The critter apparently is the first ever to be found to use a copper-containing mineral structure as part of its skeleton. The finding is remarkable first because the amount of copper detected in the jaw tip of the marine worm would normally be toxic to an organism. Second, the copper also occurs in non-mineral form in the bloodworm jaw where it may act as a sort of bridge, cross-linking long chains of fibrous proteins. And that has appealing commercial posibilities. “The marriage of protein with copper mineral as well as with bound copper ions is an intriguing concept per se but may also serve as a design prototype for new materials that need to be hard, lightweight, and durable.”