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  Peptide Mass Spectra from Micrometer-Thick Ice Films Produced with Femtosecond Pulses

Krutilin, A., Epp, S., Alejo, G. M. L., Busse, F., Gitaric, D., Schikora, H., et al. (2022). Peptide Mass Spectra from Micrometer-Thick Ice Films Produced with Femtosecond Pulses. Analytical Chemistry, 94(39), 13359-13367. doi:10.1021/acs.analchem.2c01810.

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Supporting Information: Figure S1: CAD drawing of the mass spectrometer and a schematic illustration of the beam guidance into the mass spectrometer. Figure S2: Schematic drawing of the thin-film preparation protocol. Figure S3: Schematic drawing of the home-built loading arm. Figure S4: Bright-field image of the ice thin film during different loading procedures. Figure S5: Illustration of the data acquisition strategy. Figure S6: A histogram of shot-to-shot repeatability for bradykinin signal on three substrates. Figure S7: Temperature and pressure time series in the mass spectrometer. Figure S8: Residual gas analyzer mass spectra at different points after turning off the liquid nitrogen supply. Figure S9: Threshold fluence for bradykinin signal onset on a silicon substrate during 1026 nm irradiation. Figure S10: Threshold fluence for bradykinin signal onset on a silicon substrate during 513 nm irradiation. Figure S11: Laser-induced damage on the silicon coverslip produced with different wavelengths. Figure S12: Femtosecond mass spectrometry producing a vibrant pattern of bradykinin fragment. Figure S13: Angiotensin mass spectrum produced with femtosecond pulses. Figure S14: Bright-field images of craters on a silicon wafer produced with femtosecond pulses. Figure S15: Single-shot mass spectra of 100 μM bradykinin from the same data set. Figure S16: Schematic laser profile of the fundamental and the second harmonic. Figure S17: Temperature-dependent mass spectra of fullerene C60 obtained with 1026 nm irradiation. Figure S18: Mass spectrum of endothelin
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 Creators:
Krutilin, A.1, Author           
Epp, S.2, Author           
Alejo, G. M. L.1, Author
Busse, F.1, Author           
Gitaric, D.1, Author           
Schikora, H.3, Author           
Schwoerer, H.2, Author           
Tellkamp, F.3, Author           
Affiliations:
1Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
2Ultrafast Beams, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_3255798              
3Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_2074322              

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 Abstract: We present a cryogenic mass spectrometry protocol with the capability to detect peptides in the attomole dilution range from ice films. Our approach employs femtosecond laser pulses and implements neither substrate modification nor proton donor agents in the aqueous solution, known to facilitate analyte detection in mass spectrometry. In a systematic study, we investigated the impact of temperature, substrate composition, and irradiation wavelength (513 and 1026 nm) on the bradykinin signal onset. Our findings show that substrate choice and irradiation wavelength have a minor impact on signal intensity once the preparation protocol is optimized. However, if the temperature is increased from −140 to 0 °C, which is accompanied by ice film thinning, a somehow complex picture of analyte desorption and ionization is recognizable, which has not been described in the literature yet. Under cryogenic conditions (−140 °C), obtaining a signal is only possible from isolated sweet spots across the film. If the thin ice film is between −100 and −70 °C of temperature, these sweet spots appear more frequently. Ice sublimation triggered by temperatures above −70 °C leads to an intense and robust signal onset that could be maintained for several hours. In addition to the above findings, we notice that a vibrant fragmentation pattern produced is strikingly similar with both wavelengths. Our findings suggest that while following an optimized protocol, femtosecond mass spectrometry has excellent potential to analyze small organic molecules and peptides with a mass range of up to 2.5 kDa in aqueous solution without any matrix, as employed in matrix-assisted laser desorption/ionization (MALDI) or any substrate surface modification, found in surface-assisted laser desorption/ionization (SALDI).

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Language(s): eng - English
 Dates: 2022-04-252022-08-312022-09-252022-10-04
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acs.analchem.2c01810
 Degree: -

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Title: Analytical Chemistry
  Abbreviation : Anal. Chem.
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 94 (39) Sequence Number: - Start / End Page: 13359 - 13367 Identifier: ISSN: 0003-2700
CoNE: https://pure.mpg.de/cone/journals/resource/111032812862552