Granulins are a family of growth factor proteins, which generally contain six disulfide bonds and are found in most organisms. An orthologue of granulin from the human parasitic liver fluke Opisthorchis viverrini, known as Ov-GRN-1, induces angiogenesis and accelerates wound repair. However, recombinant Ov-GRN-1 production is complex, and poses an obstacle for clinical development. We have developed peptides, based on the N-terminal region of Ov-GRN-1, that have potent in vivo wound healing activity and high oxidative folding yields. Peptides derived from Ov-GRN-1 are leads for novel wound healing therapeutics, as they are likely less immunogenic than the full-length protein and more convenient to produce. In addition to the potential therapeutic applications, these studies have identified unique folding pathways in granulins including structural roles for non-native disulfide bonds.