Granulins are a family of growth factor proteins, which generally contain six disulfide bonds and are found in most organisms.¹ They have diverse sequences and complex structure/function relationships.¹ Select examples have potential as wound healing agents making it important to improve our understanding of how granulins fold and the structural features critical for bioactivity.^2,3 Here we show, using structure-based design, chemical peptide synthesis and folding analysis, that independent folding of the N-terminal half of granulins might be a general phenomenon in the granulin family. By contrast, the C-terminal region does not fold independently in an analogous manner to the N-terminal region. We also show that the primary sequence might be more important than the three-dimensional structure for granulin bioactivity, which has implications for the design of novel wound healing agents.