Rapid renal clearance and poor oral bioavailability are major obstacles in peptide drug design. Here, we investigate an approach involving active transport to overcome these long standing challenges which is so far an under-explored pathway. The neonatal Fc receptor (FcRn) mediates transcytosis and recycling of immunoglobulin G (IgG), which results in the oral transfer of IgG from mother to infant and the long serum half-life of IgG in vivo. FcRn-binding peptides that compete with IgG binding to FcRn have been attached to the termini of proteins and resulted in fusion proteins with improved pharmacokinetic profiles. In this study, we used molecular grafting to design and synthesize a series of disulfide-rich peptides, where the FcRn-binding peptides were inserted into the intrinsically stable peptide scaffolds sunflower trypsin inhibitor-1 (SFTI-1) and kalata B1. We studied the structural features of the designed peptides using Nuclear Magnetic Resonance (NMR) spectroscopy, and showed the secondary structures of the parent scaffolds and bioactive epitopes were retained. The grafted peptides inhibited IgG binding to human FcRn in vitro with SFTI-1 analogues displaying highest affinity. In one case, we achieved a 10-fold improvement in affinity after grafting. Furthermore, a series of mono- and di-grafted SFTI-1 analogues significantly internalized into human epithelial cell monolayers expressing FcRn, compared to wild-type SFTI-1. Given the intense interest in peptides among pharmaceutical companies at present, we hope our results will stimulate researchers to explore active transport as a pathway for next-generation peptide drug design.