International Journal of Molecular Sciences

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Special Issue Information

Dear Colleagues,

An aspiration for high resolution, accuracy and sensitivity in spectroscopic and spectrometric methods can be paraphrased by the old Olympic motto of Citius, Altius, Fortius (faster, higher, stronger). Demands for high mass-resolving power and mass measurement accuracy, as well as speedy data acquisition, have been the driving forces toward advances in instrumentation that facilitate the pursuit of challenging applications of mass spectrometry. The introduction of the Fourier transform (FT) approach, development of the high-resolution time-of-flight (TOF) and ion mobility (IM) methods of ion sorting have propelled a paradigm shift to meet these challenges. FT ion cyclotron resonance (FT-ICR), Orbitrap^TM and TOF instruments are commercially available in many of today’s mass spectrometers and often in “hybrid” configurations that bring them together seamlessly with other analyzers such as quadrupoles, ion traps and IM spectrometry within one instrument. They now deliver superior performance to the delight of the broad scientific community. In addition to conventional research articles and reviews, this Special Issue (expanded in breadth from an earlier series of IJMS articles devoted to high-resolution mass spectrometry in molecular sciences) also welcomes commentaries, opinions and perspectives on the progress and applications of high-resolution mass spectrometry in broad areas of molecular sciences.

Prof. Dr. Laszlo Prokai
Guest Editor

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Keywords

antibodies
astrobiology
biomarkers
drug discovery
drug development
drug metabolism
Fourier transform
glycomics
imaging
ion cyclotron resonance
ion mobility
lipids
lipidomics
mass spectrometry
metabolomics
nucleic acids
Orbitrap
organometallics
polymers
peptides
proteins
proteomics
structural biology
structure elucidation
tandem mass spectrometry
time-of-flight

Related Special Issue

Published Papers (1 paper)

Research

12 pages, 3093 KiB

Open AccessArticle

A Mass Spectrometry Strategy for Protein Quantification Based on the Differential Alkylation of Cysteines Using Iodoacetamide and Acrylamide

by Dávid Virág, Gitta Schlosser, Adina Borbély, Gabriella Gellén, Dávid Papp, Zoltán Kaleta, Borbála Dalmadi-Kiss, István Antal and Krisztina Ludányi

Int. J. Mol. Sci. 2024, 25(9), 4656; https://doi.org/10.3390/ijms25094656 - 25 Apr 2024

Viewed by 304

Abstract

Mass spectrometry has become the most prominent yet evolving technology in quantitative proteomics. Today, a number of label-free and label-based approaches are available for the relative and absolute quantification of proteins and peptides. However, the label-based methods rely solely on the employment of stable isotopes, which are expensive and often limited in availability. Here we propose a label-based quantification strategy, where the mass difference is identified by the differential alkylation of cysteines using iodoacetamide and acrylamide. The alkylation reactions were performed under identical experimental conditions; therefore, the method can be easily integrated into standard proteomic workflows. Using high-resolution mass spectrometry, the feasibility of this approach was assessed with a set of tryptic peptides of human serum albumin. Several critical questions, such as the efficiency of labeling and the effect of the differential alkylation on the peptide retention and fragmentation, were addressed. The concentration of the quality control samples calculated against the calibration curves were within the ±20% acceptance range. It was also demonstrated that heavy labeled peptides exhibit a similar extraction recovery and matrix effect to light ones. Consequently, the approach presented here may be a viable and cost-effective alternative of stable isotope labeling strategies for the quantification of cysteine-containing proteins. Full article

(This article belongs to the Special Issue High Resolution Mass Spectrometry in Molecular Sciences: 2nd Edition)

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