The technique, published last month in Angewandte Chemie, involves the attachment of a positively charged amine group surfactant to proteins, in the case the iron storage protein ferritin, to create polymer structures that “bristle with long hairs.”

When heated to 50°C these ferritin-polymers form liquid crystals that act, according to the researchers, “like an ordinary fluid, with disorder in the positions and orientations of particles.”

The scientists believe that because the resulting “liquid” protein is more highly concentrated than those that are dissolved in water, their technique could be used to deliver “higher doses of medically useful proteins.”

Professor Stephen Mann, who led the Bristol team, said that technique “represents a possible way forward to a novel state of biomolecular matter, and could therefore have a number of important [biomedical] applications.”

The approach could be used to develop wound dressings that deliver oxygen more efficiently to a wound in order to promote healing or to improve the efficacy of enzymes that clear wounds of debris from dead cells.

Additionally, the Anglo-German team’s preliminary work on haemoglobin and myoglobin suggests that the method can be applied to a wide variety of therapeutically-important proteins.

Any technology that improves protein delivery is likely to catch the eye of the drug industry in general and the biopharmaceutical in particular.