Peptide sequencing through N-terminal phosphonylation and electrospray ionization mass spectrometry.
Peptides were phosphonylated at their N-termini by reacting with ethoxyphenylphosphinate in the presence of triethylamine and tetrachloromethane under mild conditions. The phosphonylated peptides were analyzed by tandem electrospray ionization mass spectrometry. N-Terminal phosphonylation selectively increased the intensities of b(n)-type ions relative to other ion types. The resulting simplified mass spectra clearly show the sequential loss of amino acid residues from the C-termini of peptides, providing a convenient and rapid method for peptide sequencing.
Bao
Jiangyin
J
Key Laboratory for Bioorganic Phosphorus Chemistry of Education Ministry, Department of Chemistry, Tsinghua University, Beijing 100084, P. R. China.
Ai
Huiwang
H
Fu
Hua
H
Jiang
Yuyang
Y
Zhao
Yufen
Y
Huang
Cheng
C
D063065:Organophosphonates / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D020539:Sequence Analysis, Protein / Q000379:methods*; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*
D063065:Organophosphonates; D010455:Peptides