Gel crystallises protein make-up

A crystallised protein from lobster shell

Scientists have developed a technique to crystallise proteins, which they say could aid the development of new drugs.

Proteins are the "machines" of the body, so understanding their structures and roles is crucial.

The team at Imperial College London and the University of Surrey have found a way of producing high quality crystals.

In Proceedings of the National Academy of Sciences, they say this will allow better analysis of proteins, leading to the development of targeted drugs.

It is likely to become an important part in an armoury Professor Stephen Pennington, University College Dublin

Crystallisation is the process which converts materials, such as proteins, into 3D crystals so they can be examined using X-ray crystallography.

Finding a way to do this successfully could make it much easier to examine many of the molecular pathways underpining human biology.

'Horsehair and soot'

In this study, the researchers used a substance called a nucleant, which acts as a "raft" for molecules within the protein to cling to.

Once a few have become attached, more rush to the scene, and a crystal lattice is formed.

This is another protein from a lobster shell, showing how different they can look

Various materials have been tested as nucleants - including horsehair and soot.

But nothing worked universally.

The researchers, whose work was funded by the Leverhulme Trust, decided to try a material designed by another scientist at Imperial College as a scaffold to grow stem cells on.

The porous material, called Bioglass, is made of calcium, phosphate and silicon. It is tiny - less than the size of a grain of salt - but has a series of holes which the molecules can slot in to.

Once one or two have done this, other molecules are attracted, and the lattice forms.

The scientists have found the nucleant works on many proteins.

'Not a panacea'

Professor Naomi Chayen, who led the research, said: "The first step in obtaining a good crystal is to get it to nucleate in an ordered way.

"The 'holy grail' is to find a 'universal nucleant' which would induce crystallisation of any protein.

"Although there has been considerable research in search of a universal nucleant, this is the first time we have designed one which works on a large number of materials."

She added: "To target proteins, we need to know what they look like, what they do, their size and structure."

She said treatments resulting from the research could be seen in around a decade.

The researchers plan to turn their discovery into a commercial product, using Imperial Innovations, Imperial College's technology transfer company.

Professor Stephen Pennington, of the Proteome Research Centre at University College Dublin, said the researchers were describing a "new and potentially very exciting approach".

He added: "There is clearly a long way to go to establish whether the silicon pore based nucleant is the desired universal nucleant.

"To their credit. the authors do not claim that their approach will be the universal panacea.

"Realistically it is likely to become an important part in an armoury of approaches to induce protein crystallisation."