Distinction of α- and β-aspartyl and α- and γ-glutamyl peptides by fast atom bombardment/tandem mass spectrometry

Lloyd, John R.; Cotter, Mary Lou; Ohori, David.; Doyle, Donald L.

doi:10.1002/bms.1200150707

Cited by 19 publications

(19 citation statements)

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“…Furthermore, ct-aspartic acid and/3-aspartic acid were also distinguished in the laboratory (Aubagnac et al, 1996c) by tandem mass spectrometry to detect any unwanted isomerization via a cyclic intermediate (Scheme 23) during peptide synthesis. Such differentiation has been previously studied according to other criteria (Biemann and Scoble, 1987;Lloyd et al, 1988). CAD spectra of the protonated molecules exhibited clear differences.…”

Section: Use Of Immonium Ions To Identify Proteinogenic and Non Protementioning

confidence: 96%

Some of the amino acid chemistry going on in the Laboratory of Amino Acids, Peptides and Proteins

et al. 1999

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Some of the chemistry of amino acids going on in our laboratory (Laboratoire des Amino acides Peptides et Protéines) is described as well as some mass spectrometry methodology for their characterization particularly on solid supports. Several aspects are presented including: (i) the stereoselective synthesis of natural and unnatural amino acids using 2-hydroxypinan-3-one as chiral auxiliary; (ii) the stereoselective synthesis of natural and unnatural amino acids by deracemization of alpha-amino acids via their ketene derivatives; (iii) the synthesis of alpha-aryl-alpha-amino acids via reaction of organometallics with a glycine cation; (iv) the diastereoselective synthesis of glycosyl-alpha-amino acids; (v) the synthesis of beta-amino acids using alpha-aminopyrrolidinopiperazinediones as chiral templates; (vi) the reactivity of urethane-N-protected N-carboxyanhydrides. To characterize natural and non natural amino acids through their immonium ions by mass spectrometry, some methodology is also described.

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Section: Use Of Immonium Ions To Identify Proteinogenic and Non Protementioning

confidence: 96%

Some of the amino acid chemistry going on in the Laboratory of Amino Acids, Peptides and Proteins

et al. 1999

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“…The exact Gln deamidation site(s) can be identified by using either tandem MS methods, such as collision-induced dissociation (CID), or amino acid sequencing methods 33-35. Several methods, including hydrolysis, Edman degradation, and NMR, have been developed to distinguish the isomeric α- and γ-glutamyl peptides, but each has its own disadvantages 36,37. There have also been a number of MS studies on the differentiation of the α- and γ-glutamyl residues, including the electron impact (EI) mass spectrometry,38 chemical ionization (CI) mass spectrometry,36 and fast atom bombardment (FAB)/collisional activation (CA) tandem mass spectrometry 37.…”

Section: Introductionmentioning

confidence: 99%

Glutamine Deamidation: Differentiation of Glutamic Acid and γ-Glutamic Acid in Peptides by Electron Capture Dissociation

Lin

O’Connor

2010

Anal. Chem.

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Due to its much slower deamidation rate comparing to that of asparagine (Asn), studies on glutamine (Gln) deamidation have been scarce, especially on the differentiation of its isomeric deamidation products: α- and γ-glutamic acid (Glu). It has been shown previously that electron capture dissociation (ECD) can be used to generate diagnostic ions for the deamidation products of Asn: aspartic acid (Asp) and isoaspartic acid (isoAsp). The current study explores the possibility of an extension of this ECD based method to the differentiation of the α- and γ-Glu residues, using three human crystallin peptides (αA (1-11), βB2 (4-14), and γS (52-71)) and their potentially deamidated forms as model peptides. It was found that the z•-72 ions can be used to both identify the existence and locate the position of the γ-Glu residues. When the peptide contains a charge carrier near its N-terminus, the c+57 and c+59 ions may also be generated at the γ-Glu residue. It was unclear whether formation of these N-terminal diagnostic ions is specific to the Pro-γ-Glu sequence. Unlike the Asp containing peptides, the Glu containing peptides generally do not produce diagnostic side chain loss ions, due to the instability of the resulting radical. The presence of Glu residue(s) may be inferred from the observation of a series of zn•-59 ions, although it was neither site specific, nor without interference from the γ-Glu residues. Finally, several interference peaks exist in the ECD spectra, which highlights the importance of using high performance mass spectrometers for confident identification of γ-Glu residues.

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“…Since then many other attempts have been made to distinguish isomeric forms in peptides with varying success. Some of these attempts used fast atom bombardment, and entirely relied on signature immonium ions (Aubagnac et al, 1985; Heerma & Bathelt, 1986; Lloyd et al, 1988; Kusmierz & Abramson, 1994; Castet et al, 1996). Other attempts were based on abundance ratio of b/y fragments (Gonzalez et al, 2000; Luu et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Expression of ?5 nicotinic acetylcholine receptor subunit mRNA during hippocampal and cortical development

Winzer‐Serhan

Leslie

2004

J. Comp. Neurol.

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Nicotinic acetylcholine receptors (nAChRs) are ligand-gated pentameric cation channels of alpha and beta subunits. The alpha5 subunit, when added to heteromeric complexes, alters pharmacological and physiological properties of nAChRs, which may be important during development. Here we have evaluated the pre- and postnatal expression of alpha5 subunit mRNA in rat cortex and hippocampus using highly sensitive in situ hybridization. In the cortex, alpha5 mRNA was detected in the subplate, claustrum, and endopiriform nucleus at embryonic day 18 (E18), areas with sustained expression into adulthood. Transient cortical expression was detected in numerous cells, scattered mainly in layers V and II/III, during the first 2 postnatal weeks. In the hippocampus, alpha5 transcripts first appeared in the CA1 region at E18. During postnatal development, increased hybridization signal was detected in CA1 and CA3 pyramidal neurons and granule cells of the dentate gyrus, which strongly contrasted with the low levels in the adult. Interneurons in CA1/CA3 stratum radiatum and moleculare, and in the hilus region of the dentate gyrus, strongly expressed alpha5 mRNA in postnatal and adult animals. With double in situ hybridization, co-expression of alpha5 and alpha7 mRNAs was detected in a subpopulation of hippocampal interneurons. In contrast, in the subiculum, numerous cells exhibited strong hybridization signal for alpha5 and alpha7 mRNAs, but co-expression was rarely detected. In conclusion, similar to other nAChR subunits, there is transient expression of alpha5 mRNA during cortical and hippocampal development. This expression pattern places nicotinic receptors containing the alpha5 subunit in a position to regulate glutamatergic and GABAergic transmission during the postnatal period.

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Distinction of α- and β-aspartyl and α- and γ-glutamyl peptides by fast atom bombardment/tandem mass spectrometry

Cited by 19 publications

References 4 publications

Some of the amino acid chemistry going on in the Laboratory of Amino Acids, Peptides and Proteins

Some of the amino acid chemistry going on in the Laboratory of Amino Acids, Peptides and Proteins

Glutamine Deamidation: Differentiation of Glutamic Acid and γ-Glutamic Acid in Peptides by Electron Capture Dissociation

Expression of ?5 nicotinic acetylcholine receptor subunit mRNA during hippocampal and cortical development

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