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Gluten exorphin C is an opioid peptide derived from wheat gluten. Its IC50 values are 40 μM and 13.5 μM for μ opioid and δ opioid activities in the GPI and MVD assays, respectively.

Gluten exorphin C, a novel opioid peptide, is isolated from the pepsin-trypsin-chymotrypsin digest of wheat gluten. Gluten exorphin C is evaluated its opioid activities by the GPI and MVD assays and its receptor affinities by radioreceptor assays. Its IC50s are 40 μM and 13.5 μM in the GPI and the MVD assays, respectively. Gluten exorphin C has a structure quite different from any of the endogenous and exogenous opioid peptides ever reported in that the N terminal Tyr is the only aromatic amino acid. The analogs containing Tyr-Pro-X-Ser-Leu are synthesized to study its structure-activity relationship. Peptides in which X is an aromatic amino acid or an aliphatic hydrophobic amino acid has opioid activity[1].

[1]. Fukudome S, et al. Gluten exorphin C. A novel opioid peptide derived from wheat gluten. FEBS Lett. 1993 Jan 18;316(1):17-9.

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