Matrix-assisted laser desorption/ionization of protein samples containing a denaturant at high concentration using a mid-infrared free-electron laser (MIR-FEL)

Naito, Yasuhide; Yoshihashi-Suzuki, Sachiko; Ishii, Katsunori; Kanai, Taizo; Awazu, Kunio

doi:10.1016/j.ijms.2004.11.001

Cited by 14 publications

(8 citation statements)

References 28 publications

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“…On the other hand, the IR spectrum of HSA exhibited many peaks, especially characteristic peaks at about 1650 and 1530 cm −1 (not shown). According to advanced research studies dealing with HSA, these peaks can be attributed to amide I and II peaks [12], which are sensitive to structural changes, and also resulting bonding changes of the peptide chains of HSA [13,14] as well as changes by IR-FEL for other proteins [15,16].…”

Section: Resultsmentioning

confidence: 99%

Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation

Onami

Koya

Kawasaki

et al. 2019

IJMS

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An infrared free electron laser (IR-FEL) can decompose aggregated proteins by excitation of vibrational bands. In this study, we prepared hybrid materials of protein (human serum albumin; HSA) including several new Schiff base Zn(II) complexes incorporating amino acid (alanine and valine) or dipeptide (gly-gly) derivative moieties, which were synthesized and characterized with UV-vis, circular dichroism (CD), and IR spectra. Density functional theory (DFT) and time dependent DFT (TD-DFT) calculations were also performed to investigate vibrational modes of the Zn(II) complexes. An IR-FEL was used to irradiate HSA as well as hybrid materials of HSA-Zn(II) complexes at wavelengths corresponding to imine C=N, amide I, and amide II bands. Analysis of secondary structures suggested that including a Zn(II) complex into HSA led to the structural change of HSA, resulting in a more fragile structure than the original HSA. The result was one of the characteristic features of vibrational excitation of IR-FEL in contrast to electronic excitation by UV or visible light.

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Section: Resultsmentioning

confidence: 99%

Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation

Onami

Koya

Kawasaki

et al. 2019

IJMS

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“…6 µm). Although IR-FEL has been well used to ablate biological tissues in medicine, molecular interaction of proteins with intense infrared radiation has been less studied [20][21][22] contrary to UV light [23,24].…”

Section: Introductionmentioning

confidence: 99%

Degradation of Human Serum Albumin by Infrared Free Electron Laser Enhanced by Inclusion of a Salen-Type Schiff Base Zn (II) Complex

Onami

Kawasaki

Aizawa

et al. 2020

IJMS

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A salen-type Schiff base Zn(II) complex included in human serum albumin (HSA) protein was examined by UV-Vis, circular dichroism (CD), and fluorescence (PL) spectra. The formation of the composite material was also estimated by a GOLD program of ligand–protein docking simulation. A composite cast film of HSA and Zn(II) complex was prepared, and the effects of the docking of the metal complex on the degradation of protein molecules by mid-infrared free electron laser (IR-FEL) were investigated. The optimum wavelengths of IR-FEL irradiation to be used were based on experimental FT-IR spectra and vibrational analysis. Using TD-DFT results with 6-31G(d,p) and B3LYP, the IR spectrum of Zn(II) complex could be reasonably assigned. The respective wavelengths were 1652 cm−1 (HSA amide I), 1537 cm−1 (HSA amide II), and 1622 cm−1 (Zn(II) complex C=N). Degradation of HSA based on FT-IR microscope (IRM) analysis and protein secondary structure analysis program (IR-SSE) revealed that the composite material was degraded more than pure HSA or Zn(II) complex; the inclusion of Zn(II) complex enhanced destabilization of folding of HSA.

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“…Simultaneous irradiations of a UV laser and 6-µm-band mid-IR free electron laser (FEL) enable protein samples containing a denaturant at a high concentration to be analyzed [24]. Awazu et al have demonstrated a promising technique of IR-MALDI using a DFG laser utilizing various compounds (e.g., urea) as a matrix [25].…”

Section: Introductionmentioning

confidence: 99%

Continuous Flow Atmospheric Pressure Laser Desorption/Ionization Using a 6–7-µm-Band Mid-Infrared Tunable Laser for Biomolecular Mass Spectrometry

Hiraguchi

Hazama

Senoo

et al. 2014

IJMS

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A continuous flow atmospheric pressure laser desorption/ionization technique using a porous stainless steel probe and a 6–7-µm-band mid-infrared tunable laser was developed. This ion source is capable of direct ionization from a continuous flow with a high temporal stability. The 6–7-µm wavelength region corresponds to the characteristic absorption bands of various molecular vibration modes, including O–H, C=O, CH3 and C–N bonds. Consequently, many organic compounds and solvents, including water, have characteristic absorption peaks in this region. This ion source requires no additional matrix, and utilizes water or acetonitrile as the solvent matrix at several absorption peak wavelengths (6.05 and 7.27 µm, respectively). The distribution of multiply-charged peptide ions is extremely sensitive to the temperature of the heated capillary, which is the inlet of the mass spectrometer. This ionization technique has potential for the interface of liquid chromatography/mass spectrometry (LC/MS).

show abstract

Matrix-assisted laser desorption/ionization of protein samples containing a denaturant at high concentration using a mid-infrared free-electron laser (MIR-FEL)

Cited by 14 publications

References 28 publications

Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation

Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation

Degradation of Human Serum Albumin by Infrared Free Electron Laser Enhanced by Inclusion of a Salen-Type Schiff Base Zn (II) Complex

Continuous Flow Atmospheric Pressure Laser Desorption/Ionization Using a 6–7-µm-Band Mid-Infrared Tunable Laser for Biomolecular Mass Spectrometry

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