Formation and Dissociation of Phosphorylated Peptide Radical Cations

In this study, we generated phosphoserine- and phosphothreonine-containing peptide radical cations through low-energy collision-induced dissociation (CID) of the ternary metal–ligand phosphorylated peptide complexes [CuII(terpy)pM]·2+ and [CoIII(salen)pM]·+ [pM: phosphorylated angiotensin III deriva...

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Main Authors:	Kong, Ricky P. W., Quan, Quan, Hao, Qiang, Lai, Cheuk-Kuen, Siu, Chi-Kit, Chu, Ivan K.
Format:	Online
Language:	English
Published:	Springer-Verlag 2012
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3514703/

id	pubmed-3514703
recordtype	oai_dc
spelling	pubmed-35147032012-12-05 Formation and Dissociation of Phosphorylated Peptide Radical Cations Kong, Ricky P. W. Quan, Quan Hao, Qiang Lai, Cheuk-Kuen Siu, Chi-Kit Chu, Ivan K. Research Article In this study, we generated phosphoserine- and phosphothreonine-containing peptide radical cations through low-energy collision-induced dissociation (CID) of the ternary metal–ligand phosphorylated peptide complexes [CuII(terpy)pM]·2+ and [CoIII(salen)pM]·+ [pM: phosphorylated angiotensin III derivative; terpy: 2,2':6',2''-terpyridine; salen: N,N '-ethylenebis(salicylideneiminato)]. Subsequent CID of the phosphorylated peptide radical cations (pM·+) revealed fascinating gas-phase radical chemistry, yielding (1) charge-directed b- and y-type product ions, (2) radical-driven product ions through cleavages of peptide backbones and side chains, and (3) different degrees of formation of [M – H3PO4]·+ species through phosphate ester bond cleavage. The CID spectra of the pM·+ species and their non-phosphorylated analogues featured fragment ions of similar sequence, suggesting that the phosphoryl group did not play a significant role in the fragmentation of the peptide backbone or side chain. The extent of neutral H3PO4 loss was influenced by the peptide sequence and the initial sites of the charge and radical. A preliminary density functional theory study, at the B3LYP 6-311++G(d,p) level of theory, of the neutral loss of H3PO4 from a prototypical model—N-acetylphosphorylserine methylamide—revealed several factors governing the elimination of neutral phosphoryl groups through charge- and radical-induced mechanisms. Springer-Verlag 2012-09-12 2012-12 /pmc/articles/PMC3514703/ /pubmed/22968907 http://dx.doi.org/10.1007/s13361-012-0479-7 Text en © The Author(s) 2012
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Kong, Ricky P. W. Quan, Quan Hao, Qiang Lai, Cheuk-Kuen Siu, Chi-Kit Chu, Ivan K.
spellingShingle	Kong, Ricky P. W. Quan, Quan Hao, Qiang Lai, Cheuk-Kuen Siu, Chi-Kit Chu, Ivan K. Formation and Dissociation of Phosphorylated Peptide Radical Cations
author_facet	Kong, Ricky P. W. Quan, Quan Hao, Qiang Lai, Cheuk-Kuen Siu, Chi-Kit Chu, Ivan K.
author_sort	Kong, Ricky P. W.
title	Formation and Dissociation of Phosphorylated Peptide Radical Cations
title_short	Formation and Dissociation of Phosphorylated Peptide Radical Cations
title_full	Formation and Dissociation of Phosphorylated Peptide Radical Cations
title_fullStr	Formation and Dissociation of Phosphorylated Peptide Radical Cations
title_full_unstemmed	Formation and Dissociation of Phosphorylated Peptide Radical Cations
title_sort	formation and dissociation of phosphorylated peptide radical cations
description	In this study, we generated phosphoserine- and phosphothreonine-containing peptide radical cations through low-energy collision-induced dissociation (CID) of the ternary metal–ligand phosphorylated peptide complexes [CuII(terpy)pM]·2+ and [CoIII(salen)pM]·+ [pM: phosphorylated angiotensin III derivative; terpy: 2,2':6',2''-terpyridine; salen: N,N '-ethylenebis(salicylideneiminato)]. Subsequent CID of the phosphorylated peptide radical cations (pM·+) revealed fascinating gas-phase radical chemistry, yielding (1) charge-directed b- and y-type product ions, (2) radical-driven product ions through cleavages of peptide backbones and side chains, and (3) different degrees of formation of [M – H3PO4]·+ species through phosphate ester bond cleavage. The CID spectra of the pM·+ species and their non-phosphorylated analogues featured fragment ions of similar sequence, suggesting that the phosphoryl group did not play a significant role in the fragmentation of the peptide backbone or side chain. The extent of neutral H3PO4 loss was influenced by the peptide sequence and the initial sites of the charge and radical. A preliminary density functional theory study, at the B3LYP 6-311++G(d,p) level of theory, of the neutral loss of H3PO4 from a prototypical model—N-acetylphosphorylserine methylamide—revealed several factors governing the elimination of neutral phosphoryl groups through charge- and radical-induced mechanisms.
publisher	Springer-Verlag
publishDate	2012
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3514703/
_version_	1611938140557148160

Formation and Dissociation of Phosphorylated Peptide Radical Cations

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