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Collisionally-Activated Dissociation of Peptides with a Disulfide Bond: Confirmation of the Mobile-Proton Model Based Explanation

Author(s): Younjin Lee | Han Bin Oh

Journal: Mass Spectrometry Letters
ISSN 2233-4203

Volume: 1;
Issue: 1;
Start page: 5;
Date: 2010;

Keywords: Disulfide bond | Peptides | Collisionally activated dissociation (CAD) | Mobile proton model | Tandem mass spectrometry

In the present study, collisionally-activated dissociation (CAD) experiments were performed under low energy collisionconditions in six peptides containing a disulfide bond. Fragments produced as a result of the cleavage of a disulfide bondwere obtained after CAD in four peptides (bactenecin, TGF-α, cortistantin, and linearly linked peptide, Scheme 1) with basicamino acid residues. In contrast, the CAD analysis of two peptides with no basic residue (oxytocin and tocinoic acid) rarely producedfragments indicative of cleavage of a disulfide bond. These results are consistent with the mobile proton model suggestedby the McLuckey and O’Hair groups (ref. 22 and 23); nonmobile protons sequestered at basic amino acid residues appear to promotethe cleavage of disulfide bonds.
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