Energetics and dynamics of peptide fragmentation from multiple-collision activation and surface-induced dissociation studies

Eur. J. Mass Spectrom. 10, 259–267 (2004)
DOI: 10.1255/ejms.641

Energetics and dynamics of peptide fragmentation from multiple-collision activation and surface-induced dissociation studies

Julia Laskin
Fundamental Science Directorate, Pacific Northwest National Laboratory, PO Box 999 (K8-88), Richland, WA 99352, USA. E-mail: Julia.Laskin@pnl.gov

ABSTRACT:

This account summarizes the energetics and dynamics of peptide fragmentation obtained using a new approach recently developed in our laboratory. The approach involves RRKM modeling of time- and energy-resolved tandem mass spectrometry (MS/MS) data obtained using collisional activation. We demonstrate that surface-induced dissociation (SID) on a long time-scale of Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) is perfectly suited for studying the energetics and dynamics of peptide fragmentation. The advantages provided by SID include very fast ion activation, which eliminates possible discrimination against higher-energy dissociation pathways, and efficient ”amplification” of small changes in dissociation parameters. We present a summary of results obtained for small alanine-containing peptides as well as larger peptides including angiotensin analogs and a series of peptides containing the LDIFSDF motif.

Keywords: FT-ICR mass spectrometry, SORI-CID, surface-induced dissociation (SID), peptide ions, fragmentation energetics and dynamics, kinetic shift, RRKM/QET, energy partitioning, dissociation energy, entropic factor

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