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Updated: Aug 26, 2025

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
Published on: February 27, 2019
Non-aqueous bonding of leuprorelin to ochratoxin A for peptide-based solid-phase extraction
Naoki Yamato1, Noriaki Kumagai1, Momoha Okahira1
1College of Bioscience and Biotechnology, Chubu University, Matsumoto 1200, Kasugai, Aichi 487-8501, Japan.
Abstract:
The anticancer therapeutic leuprorelin was found to have excellent affinity to the carcinogen ochratoxin A (OTA), with an equilibrium constant of 2.2 × 108 M-1 at 273 K (dissociation constant Kd = 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.
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