Researchers in the UK and Brazil have developed a method to make molecules that will help to develop a cure for a debilitating parasitic infection.

Chagas' disease is a frequently fatal condition, common in South and Central America.  It is caused by the single-celled parasite Trypanosoma cruzi. The drugs available to treat the disease are often ineffective, expensive, and highly toxic, but a cure has now been brought a step closer by a team of biochemists.

In order to complete its reproductive cycle, T. cruzi must first bind to human cells. To do this, it uses large compounds called mucins, which are synthesised by enzymes on the parasite's surface. These enzymes were the target of investigations by Robert Field at the University of East Anglia, Norwich, UK, and Ivone Carvalho at the University of São Paulo, Brazil, and colleagues. By making relatively small molecules, related to mucins, which can bind to the enzymes, the researchers aimed to understand how the enzymes operate. They hope this will help in the search for drugs that will prevent the parasite from binding and thus stop the disease taking hold.

Field and Carvalho's team made glyco-amino acids and glycopeptides related to T. cruzi mucin structures using a combination of chemical and enzymatic routes. These compounds will be critical to investigate the enzymes involved in binding of T. cruzi, which Field says is 'the first step towards drug target identification and lead generation'.

The importance of this work is echoed by Sabine Flitsch, professor of chemical biology at the Manchester Interdisciplinary Biocentre, UK. Flitsch said that the combination of biocatalysis and chemical synthesis 'is a very powerful tool in modern glycoconjugate synthesis, and the research presented by Field is a prime example of its application.'

David Barden