The protein and method by which bloodworms build their jaws have been uncovered by scientists.
Bloodworms (Glycera dibranchiate) have light skin that allows their scarlet bodily fluids to shine through and are recognised for their unusual fang-like jaws, which seem like something out of a horror movie. These are formed of protein, melanin, and copper concentrations – a feature seen nowhere else in the animal kingdom.
Scientists have identified for the first time how these worms use copper obtained from coastal sediments to construct their jaws, revealing a new multi-tasking protein detailed in a paper published in the journal Matter.
Bloodworms, like sand worms in Dune, can dig through intertidal mud (where the ocean meets the land between high and low tides) to a depth of several metres – only there’s more water and they only grow to 35 centimetres in length.
During hunting and battle, they feed by everting their proboscis – an extendable tubular sucking organ (gross) – which is armed with four black, hollow jaws that grip onto and inject paralysing venom into other unlucky species.
“These are quite nasty worms in that they are ill-tempered and readily provoked,” explains co-author Professor Herbert Waite of the University of California, Santa Barbara in the United States. “When they come into contact with another worm, they frequently fight with their copper jaws as weapons.”
Because these spikey murder tubes may pierce straight through an exoskeleton, the jaws must be sturdy and resistant enough to withstand the bloodworms’ whole five-year existence, as they only develop once.
The process of creating a bloodworm’s jaw
Waite’s group has been researching bloodworms for 20 years, but they were just recently able to watch the full chemical process that generates the jaws from beginning to end.
It is based on a protein they discovered for the first time, multi-tasking protein (MTP), a histidine and glycine amino-acid-rich complex that performs six unique roles important for jaw development and performance and serves as the principal structural protein in bloodworm jaws.
MTP attracts copper ions (Cu2+) to create a complex, then concentrates itself into a viscous, protein-rich liquid that is high in copper and phase-separates from water (think about how oil and water don’t mix).
The protein next catalyses the conversion of the amino acid derivative DOPA (dihydroxyphenylalanine – say that five times fast) into melanin polymers, after which it combines melanin and itself into thin films and fibres.
All of this contributes to the jaw’s mechanical qualities like those of fabricated metals.
The worm, like an evil genius, may exploit this method to easily synthesise a compound that, if generated in a lab, would require a difficult procedure requiring several apparatuses, solvents, and temperatures.
“We never anticipated a protein with such a simple makeup, namely glycine and histidine, to conduct so many tasks and seemingly unconnected actions,” Waite adds.
The multidisciplinary team expects that by better understanding how the bloodworm operates its self-contained processing laboratory, it may be possible to expedite portions of manufacturing that will benefit industry.
“These materials might serve as a guide for how to create and manufacture better consumer materials,” Waite adds.
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