Protein/Peptide Cleavage (Digestion)

 


The ROXY EC system shows great potential for electrochemical cleavage of the peptide bond for fast and enzyme free digestion of peptides and proteins. The mechanism is well known and the cleavage occurs specifically at the Tyrosine (Y) and Tryptophan (W) amino acid residues. Larger proteins – however require additional treatment such as acid hydrolysis at aspartic acid (D) and/or the reduction of the Disulfide Bonds to unfold the proteins and to get shorter amino acid residues, respectively, prior the oxidative electrochemical WY cleavage.

Mechanism of the electrochemical cleavage after Tyrosine (Y) and Tryptophan (W) residues.

Tyrosine containing peptides: 1000mV

Tryptophan containing peptides: 800mV


Courtesy : J. Roeser et al., Anal. Chem., 2010, 82 (18), 7556

Electrochemical Cleavage of Angiotensin I (DRVYIHPFHL)

 

Cell off: intact Angiotensin

Cell on: 900 – 1800 mV (ROXY EC system), cleavage of Angiotensin at (Y) creating the two residues DRVY and IHPFHL


Application Notes

Application Notebook


Thesis - Electrochemical Oxidation and Cleavage of Peptides in Bioanalysis, Mechanistic Aspects & Method Development Dissertation
J. Roeser; Thesis

See our support pages for a full list of recent literature