Subcritical Water Hydrolysis of Peptides: Amino Acid Side-Chain Modifications

Journal of the American Society for Mass Spectrometry
Thomas PowellHelen J Cooper

Abstract

Previously we have shown that subcritical water may be used as an alternative to enzymatic digestion in the proteolysis of proteins for bottom-up proteomics. Subcritical water hydrolysis of proteins was shown to result in protein sequence coverages greater than or equal to that obtained following digestion with trypsin; however, the percentage of peptide spectral matches for the samples treated with trypsin were consistently greater than for those treated with subcritical water. This observation suggests that in addition to cleavage of the peptide bond, subcritical water treatment results in other hydrolysis products, possibly due to modifications of amino acid side chains. Here, a model peptide comprising all common amino acid residues (VQSIKCADFLHYMENPTWGR) and two further model peptides (VCFQYMDRGDR and VQSIKADFLHYENPTWGR) were treated with subcritical water with the aim of probing any induced amino acid side-chain modifications. The hydrolysis products were analyzed by direct infusion electrospray tandem mass spectrometry, either collision-induced dissociation or electron transfer dissociation, and liquid chromatography collision-induced dissociation tandem mass spectrometry. The results show preferential oxidation of cyste...Continue Reading

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May 18, 2016·Analytical Chemistry·Thomas PowellHelen J Cooper

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Citations

Nov 11, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Arely León-LópezGabriel Aguirre-Álvarez
Jun 8, 2021·Chemical Science·Yuchen WangZheng Ouyang

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Methods Mentioned

BETA
amidation
electrophoresis

Software Mentioned

Xcalibur
Proteome Discoverer

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