Site-specific pyrolysis-induced cleavage at aspartic acid residue in peptides and proteins |
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Authors: | Zhang Shaofeng Basile Franco |
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Affiliation: | Department of Chemistry, University of Wyoming, Laramie, Wyoming 82071, USA. |
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Abstract: | A simple and site-specific nonenzymatic method based on pyrolysis has been developed to cleave peptides and proteins. Pyrolytic cleavage was found to be specific and rapid as it induced a cleavage at the C-terminal side of aspartic acid in the temperature range of 220-250 degrees C in 10 s. Electrospray ionization (ESI) mass spectrometry (MS) and tandem-MS (MS/MS) were used to characterize and identify pyrolysis cleavage products, confirming that sequence information is conserved after the pyrolysis process in both peptides and protein tested. This suggests that pyrolysis-induced cleavage at aspartyl residues can be used as a rapid protein digestion procedure for the generation of sequence-specific protein biomarkers. |
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