Citation: Jin Tang DU, Yan Mei LI, Yu Fen ZHAO, Masatoshi NAKAGAWA, Xu Rong QIN, Tadashi NEMOTO, Hiroshi NAKANISHI. MALDI-TOF Mass Spectrometry Study of the Phosphorylated Tau Peptides[J]. Chinese Chemical Letters, ;2004, 15(8): 927-930. shu

MALDI-TOF Mass Spectrometry Study of the Phosphorylated Tau Peptides

1.
Laboratory of Bioorganic Phosphorus Chemistry, Department of Chemistry, Tsinghua University, Beijing 100084;
2.
Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan

Received Date: 11 July 2003

Fund Project: The authors would like to thank the financial supports from the National Natural Science Foundation of China (No.20272032 and No.20320130046), the Teaching and Research Award Program for Outstanding Young Teachers in Higher Education Institution of MOE, P.R.C.

Fragmentation of phosphorylated Tau peptides in matrix assisted laser desorption-/ionization-time of flight-mass spectrometry (MALDI-TOF-MS) has been investigated.According to the post-source decay (PSD) in MALDI-TOF-MS, there are two different patterns of cleavage in phosphopeptides, which can be used to determine the phosphorylated site in peptides.In the synthetic tau peptides, the fragmentation at proline residue occurs strongly and this is useful to determine the structure of tau peptides.
- Mass spectrometry,
- PSD method,
- tau peptide,
- phosphorylation
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