Peptide transporters are integral membrane proteins responsible for the cellular uptake of dipeptides and tripeptides from the extracellular environment.  They play pivotal roles in nutrient absorption, antigen presentation, and cellular signaling. Despite their functions, the development of artificial peptide transporters capable of efficiently transporting charge-neutral peptides, which are highly polar and prone to aggregation, remains a challenge. Luo et al. 2025 introduced a novel class of peptide transporters involving the integration of anion and cation transport functionalities. Notably, 5F-C12, which functions as a molecular tweezer, forms a stable 1:1 complex with the charge-neutral peptide tyroserleutide, an anticancer agent currently in Phase III clinical trials. It actively facilitates its transmembrane transport by shielding it from the membrane's hydrophobic core, achieving an EC₅₀ value of 7.5 μM. 5F-C12 could enhance the peptide's bioavailability and exhibit a pronounced enhanced anticancer effect against MCF-7 breast cancer cells both in vitro and in vivo (Luo et al. 2025).