Snakin 11 (63 residues) and Snakin 22 (66 residues) are disulphide rich antimicrobial proteins isolated from solanum tuberosum (potato) tubers. Both are active (1-20 uM) against several fungal and bacterial plant pathogens but due to a lack of readily available material a detailed investigation of their structure and structural requirements for their biological activity remains undetermined. We outline the first synthesis of these intriguing peptides using native chemical ligation techniques and describe the oxidative folding of the 12 cysteines present in the linear polypeptide to afford the postulated 6 disulphide bonds. Both synthetic Snakin 1 and 2 demonstrated full biological activity when compared to natural Snakin 1 peptide. Furthermore, comparison by spectroscopic methods of the folded synthetic Snakin 2 to that obtained from natural sources suggested that these were otherwise identical.