Fibroblast growth factors (FGFs) are in clinical trials as therapies for a variety of ischemic vascular disorders. However, their short in vivo half-lives could make it difficult to maintain therapeutic levels without frequent injections. This problem has prompted Ballinger et al. to search for more stable small-molecule mimetics to replace FGF (p. 1199). Using a combination of phage display and rational design, they engineered a peptide with no homology to FGF that binds to the FGF receptor and potently reproduces FGF's biological effects (see also pp. 1157–1158).