Dublin-based scientists have taken a significant stride towards the possible development of new antibiotics to which bacteria are not resistant.

The Trinity College Dublin researchers have produced the first molecular blueprint of Globomycin - a naturally occurring antimicrobial agent which experts say could prove to be an effective infection killer into the future.

Scientists and pharmaceutical companies are under pressure to come up with replacements for the many antibiotics which are quickly becoming redundant due to bacterial resistance.

Globomycin’s potential ability to bind to and stop a particular enzyme behind the production of a protein that can lead to antibiotic resistance was marked out some time ago.

But development of new antibiotics based on it were in part hindered because scientists did not have detailed maps of the compound.

The research team in Trinity, led by Professor of Membrane Structural and Functional Biology Martin Caffrey has however cracked the structure.

X-ray crystallography records Globomycin binding

They used a technique called x-ray crystallography to record the binding of Globomycin to the LspA enzyme, allowing them to identify the binding position and map its structure.

The scientists say the blueprint, details of which are published in the journal Science, may help with the development of drugs based on Globomycin which could become important weapons in the fight against common infections.

The team say other drugs already in existence which target the same enzymes can now be examined through the prism of the blueprint to see if they can be adapted to make new broad spectrum antibiotics.

Other new narrow or bacteria specific drugs may also be developed using the new data.

"What is especially exciting is that the blueprint makes it hard to conceive bacteria developing resistance to Globomycin or newly developed analogues," Prof Caffrey said in a statement.

This, the researchers say, is because the enzyme targeted by Globomycin and the compound itself are so intertwined in structure that if the bacteria mutated in the face of the antibiotic it would probably impact its ability to function at all.