Non-aqueous bonding of leuprorelin to ochratoxin A for peptide-based solid-phase extraction.

The anticancer therapeutic leuprorelin was found to have excellent affinity to the carcinogen ochratoxin A (OTA), with an equilibrium constant of 2.2 × 10 M at 273 K (dissociation constant = 4.5 nM) when functionalized into a mesoporous polymer. Binding between the surface-bound leuprorelin and mycotoxin was corroborated with DFT calculations, and it was extended to the extraction of OTA from the heavily fatty matrices of coffee, achieving 95% recovery with improved cyclability as compared with immunoaffinity. This work presents the potential of peptide-mycotoxin interactions for durable non-aqueous extraction.