Hepcidin, a 25 amino acid peptide hormone containing a complex network of four 
disulfide bonds is the hormone regulator of iron homeostasis. Three bridges 
synthetic peptide analogs have been prepared following two synthetic strategies 
and two oxidation procedures: i) a microwave-assisted solid phase synthesis 
followed by air oxidation of the six free cysteines ii) a manual solid phase 
synthesis followed by stepwise deprotection and oxidation of cysteine pairs. All 
the peptides with different connectivities have been characterized by MALDI ToF 
spectrometry, and tested for their ability to degrade the cellular iron 
exporter, ferroportin. While linear peptides are inactive, the one-bridge and 
two-bridge peptides retaining protected cysteines by bulky substituents are 
active. Similarly, the three-bridge peptides are active irrespective of their 
disulfide connectivities.