Special Issue "Fourier Transform Mass Spectrometry in Molecular Sciences"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry, Molecular Biology and Biophysics".

Deadline for manuscript submissions: 30 October 2015

Special Issue Editor

Guest Editor
Prof. Dr. Laszlo Prokai
Department of Molecular Biology and Immunology, University of North Texas Health Science Center, 3500 Camp Bowie Boulevard, Fort Worth, Texas 76107, USA
Website: http://www.hsc.unt.edu/prokai/
Phone: +1 817 735-2206
Interests: development and use of proteomics in aging research; studying neurodegenerative diseases and cancer; with especial attention to quantitative expression profiling and oxidative stress-associated posttranslational protein modifications

Special Issue Information

Dear Colleagues,

An aspiration for high resolution, accuracy and sensitivity in spectroscopic and spectrometric methods can be paraphrased by the Olympic motto of Citius, Altius, Fortius (faster, higher, stronger). Demands for high mass-resolving power and mass-measurement accuracy have been the driving forces toward the development of instrumentation that facilitates the pursuit of challenging applications of mass spectrometry. The introduction of Fourier transform (FT) approach has enabled a paradigm-shift to meet these challenges. FT ion cyclotron resonance (FT-ICR) and Orbitrap mass analyzers, commercially available in many of today’s mass spectrometers, now deliver superior performance to the delight of the broad scientific community: the masses — when one plays with the multiple meanings of the word. In addition to conventional research articles and reviews, this special issue welcomes commentaries (including personal experience and reminiscence), opinions and perspectives about the applications of FT mass spectrometry in broad areas of the molecular sciences.

Professor Laszlo Prokai
Guest Editor

Submission

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed Open Access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1600 CHF.


Keywords

  • antibody
  • astrobiology
  • biomarkers
  • drug discovery
  • drug development
  • drug metabolism
  • Fourier transform
  • mass spectrometry
  • metabolomics
  • lipids
  • lipidomics
  • nucleic acids
  • organometallics
  • petroleomics
  • polymers
  • peptides
  • proteins
  • proteomics
  • structural biology
  • structure elucidation
  • glycomics

Published Papers (3 papers)

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Displaying article 1-3
p. 8351-8363
by , , , , , , ,  and
Int. J. Mol. Sci. 2015, 16(4), 8351-8363; doi:10.3390/ijms16048351
Received: 5 March 2015 / Revised: 2 April 2015 / Accepted: 8 April 2015 / Published: 14 April 2015
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(This article belongs to the Special Issue Fourier Transform Mass Spectrometry in Molecular Sciences)
p. 6265-6285
by , , ,  and
Int. J. Mol. Sci. 2014, 15(4), 6265-6285; doi:10.3390/ijms15046265
Received: 30 January 2014 / Revised: 22 March 2014 / Accepted: 24 March 2014 / Published: 14 April 2014
Show/Hide Abstract | PDF Full-text (1556 KB) | HTML Full-text | XML Full-text
(This article belongs to the Special Issue Fourier Transform Mass Spectrometry in Molecular Sciences)
abstract graphic
p. 24560-24580
by , , , , , ,  and
Int. J. Mol. Sci. 2013, 14(12), 24560-24580; doi:10.3390/ijms141224560
Received: 17 October 2013 / Revised: 25 November 2013 / Accepted: 26 November 2013 / Published: 17 December 2013
Show/Hide Abstract | Cited by 5 | PDF Full-text (3126 KB) | HTML Full-text | XML Full-text | Supplementary Files
(This article belongs to the Special Issue Fourier Transform Mass Spectrometry in Molecular Sciences)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Determination of oxidized phosphatidylcholines by hydrophilic interaction liquid chromatography coupled to Fourier Transform mass spectrometry
Authors: Pia Hanel, Sandra Pötz, Martina Brunner, Martin Trötzmüller, Alexander Fauland, Alexander Triebl, Ernst Lankmayr and Harald C. Köfeler
Abstract: A novel LC-MS/MS approach for analysis of oxidized phosphatidylcholines by an Orbitrap Fourier Transform mass spectrometer in positive electrospray ionization (ESI) coupled to hydrophilic interaction liquid chromatography (HILIC) was developed. This method depends on three selectivity criteria for separation and identification: retention time, exact mass at a resolution of 100.00 and collision induced dissociation (CID) fragment spectra in a linear ion trap. The process of chromatography development showed the best separation properties with a silica based Kinetex column. This type of chromatography was able to separate all major lipid classes expected in mammalian samples, yielding increased sensitivity of oxidized phosphatidylcholines over reversed phase chromatography. Identification of molecular species was achieved by exact mass on intact molecular ions and MS/MS spectra containing characteristic fragments. Due to a lack of commercially available standards, method development was performed with copper induced oxidation products of palmitoyl-arachidonoyl-phosphatidylcholine, which resulted in a plethora of lipid species oxidized at the arachidonoyl moiety. Validation of the method was done with copper oxidized human low density lipoprotein (LDL) prepared by ultracentrifugation. In these LDL samples we could identify 99 oxidized molecular phosphatidylcholine species.

Title: FOURIER TRANSFORM ION CYCLOTRON RESONANCE MASS SPECTROMETRY: The Transformation of Modern Environmental Analyses
Authors:
David Klein, Steven Bach and Fangzhi Yan
Abstract:
Fourier transformation ion cyclotron resonance mass spectrometry (FT ICR-MS) is revolutionizing how environmental analyses are performed. With the unsurpassed mass accuracy and sensitivity researchers now have a superior tool when it comes to difficult environmental analyses. Two features have really been changing the face of complex analyses. First is the ability to quickly and accurately determine the presence of unknown chemical residues in samples. For years the field has been hampered with mass spectrometric methods that were based on knowing what compounds were of interest. True unknown compounds were not possible in many methods. Secondly, the ion suppression or enhancement made quantitation problematic. Virtually every compound requires a stable isotope internal standard. These compounds are expensive and in many cases unavailable. By using the high sensitivity of the FT ICR-MS, chemists can simply dilute the sample sufficiently to minimize the ionization changes from varied matrices.

Title: Benefits of FTICR-MS in Clinical Body Fluid Profiling and Protein Identification Approaches
Author: Yuri van der Burgt
Abstract: Mass spectrometry(MS)-based clinical proteomics is a widely applied technology to find and validate protein biomarker signatures in bodily fluids such as serum or plasma. These biological samples are highly complex in terms of type of components, their concentration range and the structure identity of each species, and thus require extensive chromatographic separation or clean-up procedures. Clearly, such an elaborate and multi-step sample preparation hampers high-throughput analysis of large clinical cohorts. A final MS read-out at ultrahigh resolution enables the analysis of a more complex sample and can thus simplify upfront fractionations. To this end, Fourier transform ion cyclotron resonance (FTICR) offers superior ultrahigh resolving power with accurate and precise mass measurement of a high number of peptides and small proteins at isotopic resolution over a wide mass range. In our laboratory we have generated hundreds of “next-generation” profiles that are evaluated aiming for disease classifications. Other topics in our FTICR-MS studies include the structure characterization of proteins including post-translational modifications and recent innovation in ICR-cell technology that has resulted in similar performance at a lower magnetic field strength.

Last update: 10 June 2015

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