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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.
Molecules
November 2023
Graduate School in Nanobioscience, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan.
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.
View Article and Find Full Text PDFToward a MALDI in-source decay (ISD) method for top-down analysis of protein footprinting.
Eur J Mass Spectrom (Chichester)
October 2023
Department of Chemistry, Washington University in St Louis, St Louis, MO, USA.
Irreversible protein footprinting is a mass spectrometry-based approach in which solvent-accessible sites of a protein are modified to assess high-order protein structure. Structural insights can be gained by determining the position and extents of modification. The usual approach to obtain the "footprint" is to analyze the protein through bottom-up LC-MS/MS.
View Article and Find Full Text PDFMALDI-ISD mass spectrometry analysis as a simple and reliable tool to detect post-translational modifications of hemoglobin variants: the case of Hb Raleigh.
Clin Chem Lab Med
November 2023
National Research Council, Institute for Biomedical Research and Innovation (IRIB), Cosenza , Italy.
Tracking the disulfide rearrangement of heated lactoglobulin by matrix-assisted laser desorption/ionization-in-source decay top-down analysis.
J Mass Spectrom
May 2023
Institute for Cell Analysis, Shenzhen Bay Laboratory, Shenzhen, China.
Disulfide bond rearrangement is a common occurrence during protein analysis or treatment. A convenient and rapid method has been developed to investigate heat-induced disulfide rearrangement of lactoglobulin using matrix-assisted laser desorption/ionization-in-source decay (MALDI-ISD) technology. By analyzing heated lactoglobulin in reflectron and linear mode, we demonstrated that cysteines C66 and C160 exist as free residues other than linked ones in some protein isomers.
View Article and Find Full Text PDFRevealing charge heterogeneity of stressed trastuzumab at the subunit level.
Anal Bioanal Chem
March 2023
Department of Analytical Biochemistry, Groningen Research Institute of Pharmacy, University of Groningen, A Deusinglaan 1, 9713 AV, Groningen, The Netherlands.
Trastuzumab is known to be heterogeneous in terms of charge. Stressing trastuzumab under physiological conditions (pH 7.4 and 37 °C) increases charge heterogeneity further.
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