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Molecules
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Emerging Technologies in Biochemical Mass Spectrometry
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Emerging Technologies in Biochemical Mass Spectrometry

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Analytical Chemistry".

Deadline for manuscript submissions: closed (29 February 2024) | Viewed by 951

Special Issue Editor

Prof. Dr. Wojciech Piekoszewski

E-Mail Website
Guest Editor
Department of Analytical Chemistry, Faculty of Chemistry, Jagiellonian University, Krakow, Poland
Interests: omics chemistry; analytical chemistry; coupled HPLC; LC-MS; GC-MS; capillary electrophoresis–mass spectrometry

Special Issue Information

Dear Colleagues,

Mass spectrometry has become the leading technology deployed in ‘omics’ studies due to its high sensitivity, specificity, speed and suitability for combination with other methods. During the last few decades, there have been many developments in various aspects of mass spectrometry, including ionization methods, new principles and technology in mass analysers, sample preparation methods and data analysis algorithms.

In this Special Issue on “Emerging Technologies in Biochemical Mass Spectrometry”, we want to highlight the breadth of research and applications of mass spectrometry in biochemistry with particular emphasis on lipidomics and proteomics in the diagnosis and explanation of the mechanisms of mental, neurodegradation and metabolic diseases as well as the imaging of proteins, lipids and metals in tissues and biological structures. We also encourage submissions of both primary research papers and reviews on any aspect of mass spectrometry relating to application, method and instrumentation development as well as bioinformatics.

Prof. Dr. Wojciech Piekoszewski
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • mass spectrometry
  • lipidomics
  • metabolomics
  • proteomics
  • mass analyszer
  • bioanalysis
  • HPLC
  • LC-MS
  • GC-MS
  • high separation methods

Published Papers (1 paper)

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Research

14 pages, 8338 KiB  
Article
Transient Conformations Leading to Peptide Fragment Ion [c + 2H]+ via Intramolecular Hydrogen Bonding Using MALDI In-source Decay Mass Spectrometry of Serine-, Threonine-, and/or Cysteine-Containing Peptides
by Mitsuo Takayama
Molecules 2023, 28(23), 7700; https://doi.org/10.3390/molecules28237700 - 22 Nov 2023
Viewed by 667
Abstract
The formation of a peptide fragment ion [c + 2H]+ was examined using ultraviolet matrix-assisted laser desorption/ionization in-source decay mass spectrometry (UV/MALDI-ISD MS). Unusually, an ISD experiment with a hydrogen-abstracting oxidative matrix 4-nitro-1-naphthol (4,1-NNL) resulted in a [c + 2H]+ ion [...] Read more.
The formation of a peptide fragment ion [c + 2H]+ was examined using ultraviolet matrix-assisted laser desorption/ionization in-source decay mass spectrometry (UV/MALDI-ISD MS). Unusually, an ISD experiment with a hydrogen-abstracting oxidative matrix 4-nitro-1-naphthol (4,1-NNL) resulted in a [c + 2H]+ ion when the analyte peptides contained serine (Ser), threonine (Thr), and/or cysteine (Cys) residues, although the ISD with 4,1-NNL merely resulted in [a]+ and [d]+ ions. The [c + 2H]+ ion observed could be rationalized through intramolecular hydrogen atom transfer (HAT), like a Type-II reaction via a seven-membered conformation involving intramolecular hydrogen bonding (HB) between the active hydrogens (–OH and –SH) of the Ser/Thr/Cys residues and the backbone carbonyl oxygen at the adjacent amino (N)-terminal side residue. The ISD of the Cys-containing peptide resulted in the [c + 2H]+ ions, which originated from cleavage at the backbone N-Cα bonds far from the Cys residue, suggesting that the peptide molecule formed 16- and 22-membered transient conformations in the gas phase. The time-dependent density functional theory (TDDFT) calculations of the model structures of the Ser and Cys residues indicated that the Cys residue did not show a constructive bond interaction between the donor thiol (-SH) and carbonyl oxygen (=CO), while the Ser residue formed a distinct intramolecular HB. Full article
(This article belongs to the Special Issue Emerging Technologies in Biochemical Mass Spectrometry)
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