The unusual hydrogen-deuterium exchange of<i>α</i>-carbon protons in<i>N</i>-substituted glycine-containing peptides

Bąchor, Remigiusz; Setner, Bartosz; Kluczyk, Alicja; Stefanowicz, Piotr; Szewczuk, Zbigniew

doi:10.1002/jms.3318

Cited by 16 publications

(34 citation statements)

References 33 publications

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“…The described HDX reaction is significantly slower than HDX in functional groups containing labile protons, like amines or amides. Additionally, it is also slower than in the case of HDX at the α ‐C of sarcosine residue, which was presented by us previously .…”

Section: Resultssupporting

confidence: 52%

“…Such a procedure allowed one to observe the presence of deuterons introduced at the α ‐C. Based on our previous research , the α ‐C deuterons of N ‐methyl glycine and N ‐methyl alanine residues do not undergo the back exchange at acidic conditions.…”

Section: Resultsmentioning

confidence: 99%

“…Previously, we described an unusual hydrogen‐deuterium exchange (HDX) at the α ‐C of the sarcosine ( N ‐methyl glycine) residue in peptides incubated in 1% solution of N , N , N ‐triethylamine (TEA) in D 2 O . Sarcosine is a natural, non‐chiral N ‐methyl amino acid that plays an important role in biological systems .…”

Section: Introductionmentioning

confidence: 99%

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Convenient preparation of deuterium‐labeled analogs of peptides containing N‐substituted glycines for a stable isotope dilution LC‐MS quantitative analysis

Bąchor

Dębowski

Łęgowska

et al. 2015

Journal of Peptide Science

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N-substituted glycines constitute mimics of natural amino acids that are of great interest in the peptide-based drug development. Peptoids-oligo(N-substituted glycines) have been recently demonstrated to be highly active peptidomimetics in biological systems, resistant to proteolytic degradation. We developed a method of the deuterium labeling of peptidomimetics containing N-substituted glycine residues via H/D exchange of their α-carbon hydrogen atoms. The labeling was shown to be easy, inexpensive, and without the use of derivatization reagents or the need for a further purification. The deuterons introduced at the α-carbon atoms do not undergo a back exchange under acidic conditions during liquid chromatography mass spectrometry (LC-MS) analysis. The LC-MS analysis of a mixture of isotopologues revealed a co-elution of deuterated and nondeuterated forms of the peptidomimetics, which may be useful in the quantitative isotope dilution analysis of peptoids and other derivatives of N-substituted glycines.

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Section: Resultssupporting

confidence: 52%

Section: Resultsmentioning

confidence: 99%

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Convenient preparation of deuterium‐labeled analogs of peptides containing N‐substituted glycines for a stable isotope dilution LC‐MS quantitative analysis

Bąchor

Dębowski

Łęgowska

et al. 2015

Journal of Peptide Science

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“…The hydrogen-deuterium exchange on α-carbon of peptides containing 1-(carboxymethyl)pyridin-1-ium group was carried out according to the procedure developed in our research group for betaine derivatives45. The derivatized peptide containing 1-(carboxymethyl) 2,4,6-trimethylpyridinium and 1-(carboxymethyl) 2,4,6-triphenylpyridinium residus on the N-terminus were dissolved in D 2 O containing 1% TEA.…”

Section: Experimerntal Sectionmentioning

confidence: 99%

Peptides Labeled with Pyridinium Salts for Sensitive Detection and Sequencing by Electrospray Tandem Mass Spectrometry

Waliczek

Kijewska

Setner

et al. 2016

Sci Rep

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Mass spectrometric analysis of trace amounts of peptides may be problematic due to the insufficient ionization efficiency resulting in limited sensitivity. One of the possible ways to overcome this problem is the application of ionization enhancers. Herein we developed new ionization markers based on 2,4,6-triphenylpyridinium and 2,4,6-trimethylpyridinium salts. Using of inexpensive and commercially available pyrylium salt allows selective derivatization of primary amino groups, especially those sterically unhindered, such as ε-amino group of lysine. The 2,4,6-triphenylpyridinium modified peptides generate in MS/MS experiments an abundant protonated 2,4,6-triphenylpyridinium ion. This fragment is a promising reporter ion for the multiple reactions monitoring (MRM) analysis. In addition, the fixed positive charge of the pyridinium group enhances the ionization efficiency. Other advantages of the proposed ionization enhancers are the simplicity of derivatization of peptides and the possibility of convenient incorporation of isotopic labels into derivatized peptides.

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“…The authors have used both linear N,N,N‐trialkyl QA salts and bicyclic amines and eventually favored rigid compounds such as 1,4‐diazabicyclo[2.2.2]octane (DABCO) for their higher stability during MS/MS (no Hofmann elimination). They also noted that N‐substituted glycine‐containing peptides were amenable to hydrogen–deuterium exchange of α‐carbon protons and thus offered a comparatively simple way to prepare deuterium‐labeled peptide analogs for stable isotope dilution LC‐MS . Pyrylium‐based chemistry is also straightforward and was recognized for these purposes .…”

Section: Methodsmentioning

confidence: 99%

Pyrylium‐based dye and charge tagging in proteomics

Bayer

König

2016

Electrophoresis

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The pyrylium group is a selective reagent for ε-amino groups in proteins. In particular, for fluorescence labeling, a number of advantages over traditional N-hydroxysuccinimidyl ester chemistry were recognized such as the rapid prestaining procedure. Here, we have investigated the labeling reaction for the fluorogenic pyrylium dye Py-1 using liquid chromatography coupled to MS with the aim of determining its specificity and possible side products. Peptides containing no, one, and two lysine residue and a choice of no or one cysteine residue were labeled with Py-1 at yields > 30%. Gas phase fragmentation proved both labeling of lysine residues as well as that of the N-terminus also in peptides that contained a lysine residue. Evidence for cysteine labeling was not found, but several other products were detected such as the results of rearrangements with adjacent acidic amino acids. Apart from the use as a fluorogenic label, Py-1 recommends itself for N-terminal charge tagging as alternative to the commonly used quaternary ammonium salts. Predominantly a- and b-type ion series were observed for N-terminally labeled peptides. Further applications include chromophore tagging since the labeled product is not only fluorescent but also colored red.

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The unusual hydrogen-deuterium exchange ofα-carbon protons inN-substituted glycine-containing peptides

Cited by 16 publications

References 33 publications

Convenient preparation of deuterium‐labeled analogs of peptides containing N‐substituted glycines for a stable isotope dilution LC‐MS quantitative analysis

Convenient preparation of deuterium‐labeled analogs of peptides containing N‐substituted glycines for a stable isotope dilution LC‐MS quantitative analysis

Peptides Labeled with Pyridinium Salts for Sensitive Detection and Sequencing by Electrospray Tandem Mass Spectrometry

Pyrylium‐based dye and charge tagging in proteomics

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