Hyperdisulfide-constrained peptides are natural-occurring microproteins characterized by high cysteine content (>25%). This study aims to utilize these microproteins as hyperstable scaffolds for drug design. Here, we used β-ginkgotide-gB1 (β-gB1) from Ginkgo biloba as a model to design integrin inhibitor through epitope grafting of RGD-integrin-inhibitory-peptide (RGDi). Using alphafold2 prediction and solid-phase peptide synthesis, we designed and successfully synthesized β-gB1(RGD) by incorporating the hexapeptide RGDi into the loop2 of β-gB1. Stability assays revealed that β-gB1(RGD) is 100-time more proteolytic resistant to its linear counterpart. In conclusion, we have designed and synthesized a hyperstable microprotein with potentials to inhibit integrins for cancer metastasis.