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首页> 美国卫生研究院文献>other >Mass Spectrometry Characterization of the Thermal Decomposition/Digestion (TDD) at Cysteine in Peptides and Proteins in the Condensed Phase
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Mass Spectrometry Characterization of the Thermal Decomposition/Digestion (TDD) at Cysteine in Peptides and Proteins in the Condensed Phase

机译：热分解/消解（TDD）在半胱氨酸在肽和蛋白质的质谱法表征在冷凝相

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We report on the characterization by mass spectrometry (MS) of a rapid, reagentless and site-specific cleavage at the N-terminus of the amino acid cysteine (C) in peptides and proteins induced by the thermal decomposition at 220–250 °C for 10 seconds in solid samples. This thermally induced cleavage at C occurs under the same conditions and simultaneously to our previously reported thermally induced site-specific cleavage at the C-terminus of aspartic acid (D) (Zhang, S.; Basile, F., J. Proteome Res. 2007, 6, (5), 1700–1704). The C cleavage proceeds through cleavage of the nitrogen and α–carbon bond (N-terminus) of cysteine and produces modifications at the cleavage site with an amidation (−1 amu) of the N-terminal thermal decomposition product and a −32 amu mass change of the C-terminal thermal decomposition product, the latter yielding either an alanine or β-alanine residue at the N-terminus site. These modifications were confirmed by off-line thermal decomposition electrospray ionization (ESI)-MS, tandem MS (MS/MS) analyses and accurate mass measurements of standard peptides. Molecular oxygen was found to be required for the thermal decomposition and cleavage at C as it induced an initial cysteine thiol side chain oxidation to sulfinic acid. Similar to the thermally induced D cleavage, missed cleavages at C were also observed. The combined thermally induced digestion process at D and C, termed Thermal Decomposition/Digestion (TDD), was observed on several model proteins tested under ambient conditions and the site-specificity of the method confirmed by MS/MS.

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