The peptide hormone hepcidin is a key homeostatic regulator of iron metabolism and involved in pathological regulation of iron in response to infection, inflammation, hypoxia and anaemia. It acts by binding to the iron exporter ferroportin, causing it to be internalised and degraded. In previous work we have characterised the structure/activity relationships of  hepcidin and shown that the key residues lie in the N-terminal region of the peptide. This work contributed to the development of mini-hepcidins, which are based on the first nine amino acids of the hepcidin sequence and retain almost full in vitro activity compared to the full length peptide. In this talk I will present our work towards the synthesis of a range of analogues of mini-hepcidin analogues including N-methyl and cyclic derivatives and describe the characterisation of their structure, biological activity and physiochemical properties.