ArticleJournal of the American Society for Mass Spectrometry2009
A new copper containing MALDI matrix that yields high abundances of [peptide + Cu]+ ions.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- MALDI Matrix: Origins, Innovations, and Frontiers.Chemical reviews · 2026Review
- Small Cysteine-Rich Motif, Big Function─Metal-Driven Dimerization of the CopY C-Terminal Fragment.Inorganic chemistry · 2025Article
- Cu and Zn Interactions with Peptides Revealed by High-Resolution Mass Spectrometry.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Laserspray and matrix-assisted ionization inlet coupled to high-field FT-ICR mass spectrometry for peptide and protein analysis.Journal of the American Society for Mass Spectrometry · 2013Article
- Gold ion-angiotensin peptide interaction by mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Amino acid influence on copper binding to peptides: cysteine versus arginine.Journal of the American Society for Mass Spectrometry · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
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Abstract
The dinuclear copper complex (alpha-cyano-4-hydroxycinnamic acid (CHCA) copper salt (CHCA)(4)Cu(2)), synthesized by reacting CHCA with copper oxide (CuO), yields increased abundances of [M + xCu - (x-1)H](+) (x = 1-6) ions when used as a matrix for matrix-assisted laser desorption ionization (355 nm Nd:YAG laser). The yield of [M + xCu - (x-1)H](+) (x = 1 to approximately 6) ion is much greater than that obtained by mixing peptides with copper salts or directly depositing peptides onto oxidized copper surfaces. The increased ion yields for [M + xCu - (x-1)H](+) facilitate studies of biologically important copper binding peptides. For example, using this matrix we have investigated site-specific copper binding of several peptides using fragmentation chemistry of [M + Cu](+) and [M + 2Cu - H](+) ions. The fragmentation studies reveal interesting insight on Cu binding preferences for basic amino acids. Most notable is the fact that the binding of a single Cu(+) ion and two Cu(+) ions are quite different, and these differences are explained in terms of intramolecular interactions of the peptide-Cu ionic complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.