NDLI: Tandem Mass Spectrometric Characterization of Thiol Peptides Modified by the Chemoselective Cationic Sulfhydryl Reagent (4-Iodobutyl)Triphenylphosphonium— : Effects of a Cationic Thiol Derivatization on Peptide Fragmentation

Content Provider	Springer Nature Link
Author	Wang, Jing Zhang, Jie Arbogast, Brian Maier, Claudia S.
Copyright Year	2011
Abstract	Fixed charge chemical modifications on peptides and proteins can impact fragmentation behaviors in tandem mass spectrometry (MS/MS). In this study, we employed a thiol-specific cationic alkylation reagent, (4-iodobutyl)triphenylphosphonium (IBTP), to selectively modify cysteine thiol groups in mitochondrial proteome samples. Tandem mass spectrometric characteristics of butyltriphenylphosphonium (BTP)-modified peptides were evaluated by comparison to their carbamidomethylated (CAM) analogues using a quadrupole time-of-flight (Q-TOF) instrument under low energy collision-induced dissociation (CID) conditions. Introduction of the fixed charge modification resulted in the observation of peptide and fragment (b$_{n}$ and y$_{n}$) ions with higher charge states than those observed for CAM-modified analogues. The charged BTP moiety had a significant effect on the neighboring amide bond fragmentation products. A decrease in relative abundances of the product ions at the corresponding cleavage sites was observed compared with those from the CAM-modified derivatives. This effect was particularly noticeable when an Xxx-Pro bond was in the vicinity of a BTP group. We hypothesized that the presence of a phosphonium moiety will reduce the tendency for protonation of the proximal amide bonds in the peptide backbone. Indeed, calculations indicated that proton affinities of backbone amide bonds close to the modified cysteine residues were generally 20–50 kcal/mol lower for BTP-modified peptides than for the unmodified or CAM-modified analogues with the sequence motif -Ala-Cys-Ala$_{n}$-Ala$_{2}$-, -Ala-Cys-Ala$_{n}$-Pro-Ala-, and -Ala-Pro-Ala$_{n}$-Cys-Ala-, n = 0–3.
Starting Page	1771
Ending Page	1783
Page Count	13
File Format	PDF
ISSN	10440305
Journal	Journal of The American Society for Mass Spectrometry
Volume Number	22
Issue Number	10
e-ISSN	18791123
Language	English
Publisher	Springer-Verlag
Publisher Date	2011-07-26
Publisher Institution	The American Society for Mass Spectrometry
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Peptide fragmentation Fixed charge modification Thiol-specific modification Proline effect Organic Chemistry Biotechnology Bioinformatics Proteomics Analytical Chemistry
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Structural Biology

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Tandem Mass Spectrometric Characterization of Thiol Peptides Modified by the Chemoselective Cationic Sulfhydryl Reagent (4-Iodobutyl)Triphenylphosphonium—

Tandem mass spectrometric characterization of thiol peptides modified by the chemoselective cationic sulfhydryl reagent (4-iodobutyl)triphenylphosphonium

Chemical Derivatization of Peptide Carboxyl Groups for Highly Efficient Electron Transfer Dissociation

Peptide Dimethylation: Fragmentation Control via Distancing the Dimethylamino Group

Fast and Selective Modification of Thiol Proteins/Peptides by N-(Phenylseleno)phthalimide

A Novel Triethylphosphonium Charge Tag on Peptides: Synthesis, Derivatization, and Fragmentation

Distinguishing Aspartic and Isoaspartic Acids in Peptides by Several Mass Spectrometric Fragmentation Methods

Mass spectrometric evidence for mechanisms of fragmentation of charge-derivatized peptides

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Tandem Mass Spectrometric Characterization of Thiol Peptides Modified by the Chemoselective Cationic Sulfhydryl Reagent (4-Iodobutyl)Triphenylphosphonium— : Effects of a Cationic Thiol Derivatization on Peptide Fragmentation

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