Sequence analysis of peptides with biological activities using electrospray-Fourier trans form ion cyclotron resonance mass spectrometry

The mass spectra of five peptides with biological activities are reported. All mass spectra were recorded using a 4.7-T Fourier transform ion cyclotron resonance mass spectrometer equipped with an external electrospray source. The accurate molecular weights for the five peptides prepared by solid phase synthesis were measured as 1765.9013, 1063.5420, 1092.5254, 820.3804 and 1078.5193, respectively. All the data were obtained with the external calibration. Differences between observed and theoretical monoisotopic molecular weights were in the (0.2—1.0)×10^-6 range. The complete primary sequence for the five polypeptides were determined using the method of in-source electrospray ionization/collision induced dissociation (ESI/CID). All the intact y series ions and b series ions were obtained from various peptides respectively, thus determining the sequences of the five polypeptides. We found that the measured accurate molecular mass of sample 4 was not in agreement with that expected from the planned synthetic peptide. The sequences of sample 4 were determined through analysis. The corresponding accurate masses of b series ions and y series ions were gained, which proved that it was correct to re-determine the sequences.