Solid-phase extraction of ochratoxin A from wine based on a binding hexapeptide prepared by combinatorial synthesis
G Giraudi1, Valentina E V Ferrero, L Anfossi
1Dipartimento di Chimica Analitica, Università di Torino, Turin, Italy.
Journal of Chromatography. A
|November 13, 2007
Summary
Researchers developed a synthetic peptide that binds ochratoxin A (OTA), a mycotoxin. This peptide enables a new solid-phase extraction method for accurately quantifying OTA in wine.
Area of Science:
- Analytical Chemistry
- Food Safety
- Biochemistry
Background:
- Mycotoxins, such as ochratoxin A (OTA), pose a significant risk to food and beverage safety.
- Accurate quantification of OTA in complex matrices like wine is crucial for regulatory compliance and consumer protection.
- Existing methods for OTA detection and extraction can be costly or complex.
Purpose of the Study:
- To synthesize a hexapeptide library using combinatorial chemistry.
- To identify a specific peptide with high affinity for ochratoxin A (OTA).
- To develop a novel solid-phase extraction (SPE) method for OTA quantification in wine using the identified peptide.
Main Methods:
- Combinatorial synthesis was employed to create a hexapeptide library.
- Peptide-OTA binding affinity was assessed, identifying a Ser-Asn-Leu-His-Pro-Lys hexapeptide with K(eq)=3.4 x 10(4) M(-1).
- An immunoaffinity-like stationary phase functionalized with this peptide was developed for SPE.
Main Results:
- The Ser-Asn-Leu-His-Pro-Lys hexapeptide demonstrated significant affinity for ochratoxin A.
- The developed SPE method allowed for OTA quantification in wine down to 0.10 microg l(-1).
- High recovery rates (94.7% and 98.4% at 2.0 and 4.0 microg l(-1) OTA, respectively) were achieved without matrix interference.
Conclusions:
- A synthetic hexapeptide-based stationary phase offers an effective alternative for ochratoxin A extraction.
- This method provides a reliable and efficient approach for quantifying OTA in wine samples.
- The performance of this novel SPE method is comparable to established immunoaffinity extraction techniques.

