Chem. J. Chinese Universities ›› 2020, Vol. 41 ›› Issue (7): 1505.doi: 10.7503/cjcu20200262

• Analytical Chemistry • Previous Articles     Next Articles

Assignment of Polypeptide Disulfide Bonds by Chemical Cleavage and Bio-mass Spectrometry

WANG Xiaoyu,YAN Guoquan,ZHOU Xinwen*(),YANG Pengyuan*()   

  1. Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China
  • Received:2020-05-08 Online:2020-07-10 Published:2020-06-15
  • Contact: Xinwen ZHOU,Pengyuan YANG E-mail:zhouxinwen@fudan.edu.cn;pyyang@fudan.edu.cn
  • Supported by:
    Professional Technical Service Platform for Critical Diseases in Shanghai, China(18DZ2292900)

Abstract:

Disulfide bridges are important chemical bonds closely related to the structure and function of peptides and proteins. There may be multiple pairs of disulfide bonds when more than two cysteines existed in a peptide. Quickly and accurately assignment is crucial for evaluating the relationship between structure and function of peptide. In this paper, a comprehensive chemical cleavage and mass spectrometry method was developed to assign three pairs of disulfide bonds in Linalotide. Linalotide disulfide bonds were Cys1-Cys6, Cys2-Cys10 and Cys5-Cys13 by mapping tandem mass spectrum of specific peptides. This method provides a new idea for the study of peptide disulfide bond location.

Key words: Assignment of disulfide bond, Chemical cleavage, Bio-mass spectrometry, Linaclotide

CLC Number: 

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