## Abstract Mammalian ribonucleotide reductase (mRR) is a potential target for cancer intervention. A series of lactamβbridged cyclic peptide inhibitors (1β9) of mRR have been synthesized and tested in previous work. These inhibitors consist of cyclic and linear regions, causing their mass spectral
Peptide sequencing through N-terminal phosphonylation and electrospray ionization mass spectrometry
β Scribed by Jiangyin Bao; Huiwang Ai; Hua Fu; Yuyang Jiang; Yufen Zhao; Cheng Huang
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 125 KB
- Volume
- 40
- Category
- Article
- ISSN
- 1076-5174
- DOI
- 10.1002/jms.850
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β¦ Synopsis
Abstract
Peptides were phosphonylated at their Nβtermini 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. NβTerminal phosphonylation selectively increased the intensities of b~n~βtype ions relative to other ion types. The resulting simplified mass spectra clearly show the sequential loss of amino acid residues from the Cβtermini of peptides, providing a convenient and rapid method for peptide sequencing. Copyright Β© 2005 John Wiley & Sons, Ltd.
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