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Updated: Jun 27, 2026

Determination of the Gas-phase Acidities of Oligopeptides
Published on: June 24, 2013
Comparison of LID versus CID activation modes in tandem mass spectrometry of peptides
Nawar Shenar1, Nicolas Sommerer, Jean Martinez
1Institut des Biomolécules Max Mousseron, UMR 5247 CNRS-Universités Montpellier 1 et 2, Bâtiment Chimie (17), Université Montpellier 2, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France.
Abstract:
We report our contribution to the systematic investigation of peptide fragmentations performed on high-performance Tof equipment, operating in MS and MS/MS modes, such as ESI-QqTof and MALDI-Tof/Tof instruments that are commonly available today in proteomic laboratories. Whereas the former analyzer's configuration provides low-energy collision-induced dissociations (CID), the latter allows tunable activation methods of the selected parent ion to induce either metastable laser-induced dissociations (LID) or high-energy CID ('gas on spectra LID'). Fragmentation of the monoprotonated ion of 53 peptides (FW 807-2853 g/mol) was undertaken upon low-energy CID on an ESI-QTof mass spectrometer (Waters) as well as high-energy CID and LID conditions on a MALDI Ultraflex mass spectrometer (Bruker). Systematic comparison of MS/MS spectra provided useful information on the performance of each piece of equipment for efficient peptide sequencing and also insights into the observed fragmentation behaviors.
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