ArticleJournal of the American Society for Mass Spectrometry2014
Insights into the binding sites of organometallic ruthenium anticancer compounds on peptides using ultra-high resolution mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Binding Modes of a Cytotoxic Dinuclear Copper(II) Complex with Phosphate Ligands Probed by Vibrational Photodissociation Ion Spectroscopy.Inorganic chemistry · 2023Article
- Determination of Relative Stabilities of Metal-Peptide Bonds in the Gas Phase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Top-down mass spectrometry reveals multiple interactions of an acetylsalicylic acid bearing Zeise's salt derivative with peptides.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Metal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Native electrospray mass spectrometry approaches to probe the interaction between zinc and an anti-angiogenic peptide from histidine-rich glycoprotein.Scientific reports · 2018Article
- Small Molecule Catalysts with Therapeutic Potential.Molecules (Basel, Switzerland) · 2018Review
- Expression proteomics study to determine metallodrug targets and optimal drug combinations.Scientific reports · 2017Article
- Editorial of Special Issue Ruthenium Complex: The Expanding Chemistry of the Ruthenium Complexes.Molecules (Basel, Switzerland) · 2015Article
- The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Protein science : a publication of the Protein Society · 2015Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The binding sites of two ruthenium(II) organometallic complexes of the form [(η(6)-arene)Ru(N,N)Cl](+), where arene/N,N = biphenyl (bip)/bipyridine (bipy) for complex AH076, and biphenyl (bip)/o-phenylenediamine (o-pda) for complex AH078, on the peptides angiotensin and bombesin have been investigated using Fourier transform ion cyclotron resonance (FTICR) mass spectrometry. Fragmentation was performed using collisionally activated dissociation (CAD), with, in some cases, additional data being provided by electron capture dissociation (ECD). The primary binding sites were identified as methionine and histidine, with further coordination to phenylalanine, potentially through a π-stacking interaction, which has been observed here for the first time. This initial peptide study was expanded to investigate protein binding through reaction with insulin, on which the binding sites proposed are histidine, glutamic acid, and tyrosine. Further reaction of the ruthenium complexes with the oxidized B chain of insulin, in which two cysteine residues are oxidized to cysteine sulfonic acid (Cys-SO3H), and glutathione, which had been oxidized with hydrogen peroxide to convert the cysteine to cysteine sulfonic acid, provided further support for histidine and glutamic acid binding, respectively.
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Registered trials
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