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

作　　者：HE Meiyu XU Jiaxi HE Xiaoran Tak Wah Dominic Chan Rebecca L.C.Lau 

机构地区：[1]Department of Chemistry,Peking University,Beijing 100871,China [2]Beijing Mass Spectrometry Center,Beijing 100080,China [3]Department of Chemistry,The Chinese University of Hong Kong,Shatin,N.T.,Hong Kong,China

出　　处：《Chinese Science Bulletin》2001年第15期1281-1285,共5页

基　　金：This work was supported by the National Natural Science Foundation of China (Grant No. 29775004).

摘　　要：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 polypep-tides 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 meas-ured accurate molecular mass of sample 4 was not in agreement with that expected from the plannedThe 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 insource 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 redetermine the sequences.

关 键 词：sequence peptide with BIOLOGICAL activity Fourier transform ion CYCLOTRON resonance mass SPECTROMETRY ELECTROSPRAY collision-induced dissociation. 

分 类 号：Q503[生物学—生物化学]