Neutral loss of amino acid residues from protonated peptides in collision‐induced dissociation generates N‐ or C‐terminal sequence ladders

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Abstract
The widespread occurrence of the neutral loss of one to six amino acid residues as neutral fragments from doubly protonated tryptic peptides is documented for 23 peptides with individual sequences. Neutral loss of amino acids from the N‐terminus of doubly charged tryptic peptides results in doubly charged y‐ions, forming a ladder‐like series with the ions [M + 2H]2+ = ymax2+, ymax − 12+, ymax − 22+, etc. An internal residue such as histidine, proline, lysine or arginine appears to favor this type of fragmentation, although it was sometimes also observed for peptides without this structure. For doubly protonated non‐tryptic peptides with one of these residues at or near the N‐terminus, we observed neutral loss from the C‐terminus, resulting in a doubly charged b‐type ion ladder. The analyses were performed by Q‐TOF tandem mass spectrometry, facilitating the recognition of neutral loss ladders by their 2+ charge state and the conversion of the observed mass differences into reliable sequence information. It is shown that the neutral loss of amino acid residues requires low collision offset values, a simple mechanistic explanation based on established fragmentation rules is proposed and the utility of this neutral loss fragmentation pathway as an additional source for dependable peptide sequence information is documented. Copyright © 2003 John Wiley & Sons, Ltd.

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