Overexpression of fibroblast growth factor receptor 1 ( FGFR 1) is a common aberration in lung and breast cancers and has necessitated the design of drugs targeting FGFR 1‐dependent downstream signaling and FGFR 1 ligand binding. To date, the major group of drugs being developed for treatment of FGFR 1‐dependent cancers are small‐molecule tyrosine kinase inhibitors; however, the limited specificity of these drugs has led to increasing attempts to design molecules targeting the extracellular domain of FGFR 1. Here, we used the phage display technique to select cyclic peptides F8 ( ACSLNHTVNC ) and G10 ( ACSAKTTSAC ) as binders of the fibroblast growth factor 1 ( FGF 1)– FGFR 1 interface. ELISA and in vitro cell assays were performed to reveal that cyclic peptide F8 is more effective in preventing the FGF 1– FGFR 1 interaction, and also decreases FGF 1‐induced proliferation of BA /F3 FGFR 1c cells by over 40%. Such an effect was not observed for BA /F3 cells lacking FGFR 1. Therefore, cyclic peptide F8 can act as a FGF 1– FGFR 1 interaction antagonist, and may be suitable for further development for potential use in therapies against FGFR 1‐expressing cancer cells.