Novel method for [M + Cu]+ ion formation by matrix-assisted laser desorption ionization

Shields, Sharon J.; Bluhm, Brian K.; Russell, David H.

doi:10.1016/s1387-3806(98)14256-2

Cited by 32 publications

(34 citation statements)

References 45 publications

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“…In contrast, cationization assists ionization of analytes that are difficult to ionize by other ionization pathways. Therefore, salts of metal cations such as Li + , Cu 2+ , and Ag + are often added to MALDI samples to enhance signal or suppress cationization by Na + and K + [31,34,35]. Several other mechanical methods, including a postcrystallization wash [36] layered deposition of matrix and analyte [37], and the use of liquid matrices (ionic liquids containing matrix anions) [38], have also been proposed and tested to minimize cationization in MALDI.…”

Section: Introductionmentioning

confidence: 99%

Sodium Cation Affinities of Commonly Used MALDI Matrices Determined by Guided Ion Beam Tandem Mass Spectrometry

Chinthaka¹,

Rodgers²

2012

J. Am. Soc. Mass Spectrom.

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The sodium cation affinities of six commonly used MALDI matrices are determined here using guided ion beam tandem mass spectrometry techniques. The collision-induced dissociation behavior of six sodium cationized MALDI matrices, Na + (MALDI), with Xe is studied as a function of kinetic energy. The MALDI matrices examined here include: nicotinic acid, quinoline, 3-aminoquinoline, 4-nitroaniline, picolinic acid, and 3-hydroxypicolinic acid. In all cases, the primary dissociation pathway corresponds to endothermic loss of the intact MALDI matrix. The cross section thresholds are interpreted to yield zero and 298 K Na + −MALDI bond dissociation energies (BDEs), or sodium cation affinities, after accounting for the effects of multiple ionneutral collisions, the kinetic and internal energy distributions of the reactants, and dissociation lifetimes. Density functional theory calculations at the B3LYP/6-311+G(2d,2p)//B3LYP/6-31G* and MP2(full)/6-311+G(2d,2p)//B3LYP/6-31G* levels of theory are used to characterized the structures and energetics for these systems. The calculated BDEs exhibit very good agreement with the measured values for most systems. The experimental and theoretical Na + −MALDI BDEs determined here are compared with those previously measured by cation transfer equilibrium methods.

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Section: Introductionmentioning

confidence: 99%

Sodium Cation Affinities of Commonly Used MALDI Matrices Determined by Guided Ion Beam Tandem Mass Spectrometry

Chinthaka¹,

Rodgers²

2012

J. Am. Soc. Mass Spectrom.

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“…More abundant formation of gold ion-angiotensin complexes are detected as compare to the complex formation of Zn ion and Cu ion. In addition, CID data reveals many possible gold ion binding sites in the vicinity of Cys, His, and Arg of peptides, which is somewhat different from Zn ion (His is the preferred anchoring site) [48] and Cu ion (Arg is the preferred anchoring) [34,41].…”

mentioning

confidence: 97%

“…With the development of gentle ionization techniques such as ESI [29,30] and MALDI [31,32] for transferring peptides/proteins into the gas phase without detrimental effects on their integrity, mass spectrometry has been used successfully to characterize metal cation (such as calcium, cadmium, cobalt, copper, iron, magnesium, mercury, nickel, potassium, sodium, and zinc) peptide/protein interactions [33][34][35][36][37][38][39][40][41][42][43][44][45][46]. Data reveals some general findings such as various metal ions may interact differently to a peptide sequence [33,47], and the metal cation-peptide/protein bond is believed to be noncovalent [33].…”

mentioning

confidence: 99%

“…Many MS studies suggest that the Cupeptide ions by MALDI is formed by a reductive process which produces primarily Cu(I)-peptide ions, whereas ESI process yields almost exclusively Cu(II)-peptide ions unless a solvable copper emitter is used [34]. Collision induced dissociation (CID), a well established tandem mass spectrometry experiment, which produces the information of the sequence and metal ion binding sites of a peptide, of Zn ionand Cu ion-angiotensin peptide complexes [34,41,48] indicate that zinc and copper interaction sites are in the neighborhood of the His and Arg residues, respectively. In addition, there are some MS studies on the gold-protein complexes [14,28,33,[49][50][51][52], disulfide bridge cleavage of gold(I) cationized peptides [53,54], and characterization of synthetic pure gold-peptide complexes [21][22][23][24][25][26][27].…”

mentioning

confidence: 99%

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Gold Ion–Angiotensin Peptide Interaction by Mass Spectrometry

Lee

Jayathilaka

Gupta

et al. 2012

J. Am. Soc. Mass Spectrom.

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Stimulated by the interest in developing gold compounds for treating cancer, gold ionangiotensin peptide interactions are investigated by mass spectrometry. Under the experimental conditions used, the majority of gold ion-angiotensin peptide complexes contain gold in the oxidation states I and III. Both ESI-MS and MALDI-TOF MS detect singly/multiply charged ions for mononuclear/multinuclear gold-attached peptides, which are represented as [peptide+a Au (I)+b Au(III)+(e -a -3b) H] e+ , where a,b≥0 and e is charge. ESI-MS data shows singly/multiply charged ions of Au(I)-peptide and Au(III)-peptide complexes. This study reveals that MALDI-TOF MS mainly detects singly charged Au(I)-peptide complexes, presumably due to the ionization process. The electrons in the MALDI plume seem to efficiently reduce Au(III) to Au(I). MALDI also tends to enhance the higher polymeric forms of gold-peptide complexes regardless of the laser power used. Collision-induced dissociation experiments of the mononuclear and dinuclear gold-attached peptide ions for angiotensin peptides show that the gold ion (a soft acid) binding sites are in the vicinity of Cys (a soft ligand), His (a major anchor of peptide for metal ion chelation), and the basic residue Arg. Data also suggests that the abundance of gold-attached peptides increases with higher gold concentration until saturation, after which an increase in gold ion concentration leads to the aggregation and/or precipitation of gold-bound peptides.

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“…Metallic copper has been also used to generate Cu + ions in the gas-phase by direct ionization of the metal in matrix-assisted laser desorption ionization (MALDI) and fast atom bombardment (FAB) [11][12][13]. In ESI-MS, the electrode used to apply the high-voltage acts as an anode when operating in the positive ionization mode [14].…”

Section: Introductionmentioning

confidence: 99%

Electrochemical generation of Cu(I) complexes in aqueous solutions studied by on-line mass spectrometry

Prudent

Roussel

2007

Electrochemistry Communications

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Taking advantage of the electrochemical aspects of electrospray ionization (ESI) sources in positive ionization mode mass spectrometry (MS), aqueous copper complexes are electrogenerated using sacrificial copper electrodes. When using 8-hydroxyquinoline or bathocuproine, two chelating agents for Cu 2+ and Cu + ions, respectively, the electrodissolution of copper leads to the formation of the respective complexes that are then analyzed by MS. This electrochemical generation of copper(I) complexes offers a direct route to synthesize Cu + complexes in aqueous solutions.

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Novel method for [M + Cu]+ ion formation by matrix-assisted laser desorption ionization

Cited by 32 publications

References 45 publications

Sodium Cation Affinities of Commonly Used MALDI Matrices Determined by Guided Ion Beam Tandem Mass Spectrometry

Sodium Cation Affinities of Commonly Used MALDI Matrices Determined by Guided Ion Beam Tandem Mass Spectrometry

Gold Ion–Angiotensin Peptide Interaction by Mass Spectrometry

Electrochemical generation of Cu(I) complexes in aqueous solutions studied by on-line mass spectrometry

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