Granulins are a family of protein growth factors which are involved in a range of biological functions, including wound repair, inflammation and tumour growth. They typically contain six disulfide bonds; however, significant sequential, structural and bioactivity variations exist. Our overall goal is to enhance the understanding of the folding and structure/function relationships of granulins. This has been achieved using peptide synthesis with FMOC chemistry to produce a range of naturally occurring and engineered peptides. The structures have been analysed using NMR spectroscopy and the activity assessed using cell-based assays. The insight gained from this study is likely to enhance efforts to develop granulin as a novel wound healing agent, as it has recently been shown that a granulin peptide derived from the human liver fluke, Opisthorchis viverrini, has wound healing properties and analogues of this protein are being developed as potential wound healing agents. Despite the recent advances in elucidating granulin structure/function relationships, it is becoming apparent that there are still many unanswered questions regarding the folding and bioactivity of granulins. Our current study provides insight into the structure/function relationships of zebrafish granulin. Specifically, this study helps to determine independent folding motifs present in the granulin peptides, and insight into structural features important for bioactivity.