Investigation of the protonation site in the dialanine peptide by infrared multiphoton dissociation spectroscopy

Lucas, Bruno; Grégoire, Gilles; Lemaire, Joël; Maı̂tre, Philippe; Ortéga, J.M.; Rupenyan, Alisa; Reimann, Bernd; Schermann, J. P.; Desfrançois, C.

doi:10.1039/b316053j

Cited by 88 publications

(129 citation statements)

References 22 publications

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“…In the recent years, several investigations have employed soft ionization techniques, such as matrix-assisted laser desorption ionization (MALDI) [104][105][106][107], electrospray ionization (ESI) [108,109], and collision-induced dissociation (CID) [110][111][112][113][114], to study the ionization and fragmentation of different amino acids and small peptides in the gas phase. Gas-phase investigations of LEE-induced damage to protein subunits have been reported for the amino acids alanine [115], tyrosine [116], glycine [117,118], proline [119,120], cysteine [121], and serine [122,123], as well as small peptides, such as dialanine [124] and amino acid esters [125].…”

Section: Lees Interaction With Protein Building Blocksmentioning

confidence: 99%

Transient Anions in Radiobiology and Radiotherapy: From Gaseous Biomolecules to Condensed Organic and Biomolecular Solids

Alizadeh¹,

Ptasińska²,

Sanche³

2016

Radiation Effects in Materials

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This chapter focuses on the fundamental processes that govern interactions of lowenergy (1-30 eV) electrons with biological systems. These interactions have been investigated in the gas phase and within complex arrangements in the condensed phase. They often lead to the formation of transient molecular anions (TMAs), and their decay by autoionization or dissociation accompanied by bond dissociation. The damage caused to biomolecules via TMAs is emphasized in all sections. Such damage, which depends on a large number of factors, including electron energy, molecular environment, and type of biomolecule, and its physical and chemical interactions with radiosensitizing agents are extensively discussed. A majority of recent findings resulting from experimental and theoretical endeavors are presented. They encompass broad research areas to elucidate important roles of TMAs in irradiated biological systems, from the molecular level to nanoscale cellular dimensions. Fundamental aspects of TMA formation are stressed in this chapter, but many practical applications in a variety of radiation-related fields such as radiobiology and radiotherapy are addressed.

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Section: Lees Interaction With Protein Building Blocksmentioning

confidence: 99%

Transient Anions in Radiobiology and Radiotherapy: From Gaseous Biomolecules to Condensed Organic and Biomolecular Solids

Alizadeh¹,

Ptasińska²,

Sanche³

2016

Radiation Effects in Materials

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“…14 In recent years there have been several investigations of the ionization and fragmentation of small and medium-size peptides and proteins using soft ionization techniques such as matrix-assisted laser desorption ionization (MALDI), [15][16][17][18] electrospray ionization (ESI), 19,20 and collision induced dissociation (CID). [21][22][23][24][25][26] Moreover, amino acid clustering and especially the role of chiral discrimination in the formation of such clusters has been studied by mass spectrometry. [27][28][29][30][31] However, to date only a few studies of the interaction of low energy electrons with small peptides isolated in the gas phase have been carried out.…”

Section: Introductionmentioning

confidence: 99%

Bond dissociation of the dipeptide dialanine and its derivative alanine anhydride induced by low energy electrons

Alizadeh

Gschliesser

Bartl

et al. 2011

The Journal of Chemical Physics

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Dissociative electron attachment to dialanine and alanine anhydride has been studied in the gas phase utilizing a double focusing two sector field mass spectrometer. We show that low-energy electrons (i.e., electrons with kinetic energies from near zero up to 13 eV) attach to these molecules and subsequently dissociate to form a number of anionic fragments. Anion efficiency curves are recorded for the most abundant anions by measuring the ion yield as a function of the incident electron energy. The present experiments show that as for single amino acids (M), e.g., glycine, alanine, valine, and proline, the dehydrogenated closed shell anion (M-H) − is the most dominant reaction product. The interpretation of the experiments is aided by quantum chemical calculations based on density functional theory, by which the electrostatic potential and molecular orbitals are calculated and the initial electron attachment process prior to dissociation is investigated.

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“…Experimentally, sodium and/or potassium ion complexes of both Ala [12] and Phe [16] have been characterized by IRMPD spectroscopy, and we can also note examples of structural studies using this technique with other amino acid complexes. [1,9,24] The recent IRMPD spectroscopic study of M + Trp complexes [25] is particularly helpful in interpretation of complexes involving cation-π interactions, through the characterization of the mixtures of conformers present in the Trp systems.…”

Section: Introductionmentioning

confidence: 99%

Alkali Metal Complexes of the Dipeptides PheAla and AlaPhe: IRMPD Spectroscopy

2008

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Complexes of PheAla and AlaPhe with alkali metal ions Na + and K + were generated by electrospray ionization, isolated in the Fourier-transform ion cyclotron resonance (FT-ICR) ion trapping mass spectrometer, and investigated spectroscopically by infrared multiple-photon dissociation (IRMPD) using light from the FELIX free electron laser over the mid-infrared range from 500 to 1900 cm -1 . Conclusions about structural features of the complexes were drawn by comparison with predicted spectra and relative free energies calculated by DFT for a number of candidate conformers.Combining spectroscopic and energetic results, it is established that the metal ion is always chelated by the amide carbonyl oxygen, and that the C-terminal hydroxyl does not complex the metal ion and is in the endo conformation. It is also likely that the aromatic ring of Phe always chelates the metal ion in a cation-π binding configuration. Along with the amide CO and ring chelation sites, a third Lewis-basic group almost certainly chelates the metal ion, giving a threefold chelation geometry. This third site may be either the Cterminal carbonyl oxygen, or the N-terminal amino nitrogen. From the spectroscopic and computational evidence, a slight preference was given to the carbonyl group, in an RO a O t chelation pattern, but the amino group is almost equally likely (particularly for 2

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Investigation of the protonation site in the dialanine peptide by infrared multiphoton dissociation spectroscopy

Cited by 88 publications

References 22 publications

Transient Anions in Radiobiology and Radiotherapy: From Gaseous Biomolecules to Condensed Organic and Biomolecular Solids

Transient Anions in Radiobiology and Radiotherapy: From Gaseous Biomolecules to Condensed Organic and Biomolecular Solids

Bond dissociation of the dipeptide dialanine and its derivative alanine anhydride induced by low energy electrons

Alkali Metal Complexes of the Dipeptides PheAla and AlaPhe: IRMPD Spectroscopy

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