The low energy collision-induced dissociation of fixed-charge derivatives [tris(2,4,6-trimethoxyphenyl)phosphonium] of peptides was investigated using an electrospray ion trap mass spectrometer. The fixed charge directed the fragmentation pattern and generated solely N-terminal fragments with minimal internal rearrangement, regardless of the presence and position of basic amino acids in the peptide chain. Generally only b-type ions, accompanied by less intense a-type ions, were observed, depending on the collision energy. It was observed that the fixed charge controlled the fragmentation beyond typical MS/MS, and thus the capacity of the ion trap to perform multiple stage fragmentation (MS(n)) was found particularly useful for obtaining the complete sequence information of the peptides.
Copyright 1999 John Wiley & Sons, Ltd.