Special Issue "Recent Advancements in Analysis of Biomolecules with Separation Technologies"

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A special issue of Separations (ISSN 2297-8739).

Deadline for manuscript submissions: closed (30 June 2014)

Special Issue Editor

Guest Editor
Dr. Wenwan Zhong

Department of Chemistry, University of California, Riverside, CA 92508, USA
Website | E-Mail
Interests: capillary electrophoresis; flow field flow fractionation; molecular interaction; biosening; nano-bio interface

Special Issue Information

Dear Colleagues,

Separation technologies have advanced significantly in the past decade. In particular, development of new techniques as well as application/improvement of existing techniques for analysis of small compounds important for biological processes, macromolecules like nucleic acids, proteins, carbohydrates, and lipids, and bioparticles such as cell organelles, viruses, and bacteria, have provided great assistance to the exploration of systems biology.  Therefore, this special issue will be devoted to the new development, technology advancement, and novel application of separation technology for study of biomolecules and/or their functions. With this issue, we hope to highlight the significant contribution of separation science towards understanding how biosystems function, and to illuminate the future direction of bioseparation for imposing higher impacts to our society.

Dr. Wenwan Zhong
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. Separations is an international peer-reviewed Open Access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. For the first couple of issues the Article Processing Charge (APC) will be waived for well-prepared manuscripts. English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.


Keywords

  • separation
  • biologically relevant molecules
  • analysis

Published Papers (4 papers)

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Research

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Open AccessArticle Electrophoretic Extraction and Proteomic Characterization of Proteins Buried in Marine Sediments
Chromatography 2014, 1(4), 176-193; doi:10.3390/chromatography1040176
Received: 1 July 2014 / Revised: 11 September 2014 / Accepted: 18 September 2014 / Published: 13 October 2014
PDF Full-text (646 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Proteins are the largest defined molecular component of marine organic nitrogen, and hydrolysable amino acids, the building blocks of proteins, are important components of particulate nitrogen in marine sediments. In oceanic systems, the largest contributors are phytoplankton proteins, which have been tracked from
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Proteins are the largest defined molecular component of marine organic nitrogen, and hydrolysable amino acids, the building blocks of proteins, are important components of particulate nitrogen in marine sediments. In oceanic systems, the largest contributors are phytoplankton proteins, which have been tracked from newly produced bloom material through the water column to surface sediments in the Bering Sea, but it is not known if proteins buried deeper in sediment systems can be identified with confidence. Electrophoretic gel protein extraction methods followed by proteomic mass spectrometry and database searching were used as the methodology to identify buried phytoplankton proteins in sediments from the 8–10 cm section of a Bering Sea sediment core. More peptides and proteins were identified using an SDS-PAGE tube gel than a standard 1D flat gel or digesting the sediment directly with trypsin. The majority of proteins identified correlated to the marine diatom, Thalassiosira pseudonana, rather than bacterial protein sequences, indicating an algal source not only dominates the input, but also the preserved protein fraction. Abundant RuBisCO and fucoxanthin chlorophyll a/c binding proteins were identified, supporting algal sources of these proteins and reinforcing the proposed mechanisms that might protect proteins for long time periods. Some preserved peptides were identified in unexpected gel molecular weight ranges, indicating that some structural changes or charge alteration influenced the mobility of these products during electrophoresis isolation. Identifying buried photosystem proteins suggests that algal particulate matter is a significant fraction of the preserved organic carbon and nitrogen pools in marine sediments. Full article
Open AccessArticle Adaptation of a High-Pressure Liquid Chromatography System for the Measurement of Viscosity
Chromatography 2014, 1(2), 55-64; doi:10.3390/chromatography1020055
Received: 27 January 2014 / Revised: 10 March 2014 / Accepted: 17 March 2014 / Published: 26 March 2014
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Abstract
The state-of-the-art instruments for the determination of viscosity of liquids typically require a significant amount of sample, and have relatively low throughput due to manual and sequential measurements. In this study, it was demonstrated that the pressure generated by the flow of viscous
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The state-of-the-art instruments for the determination of viscosity of liquids typically require a significant amount of sample, and have relatively low throughput due to manual and sequential measurements. In this study, it was demonstrated that the pressure generated by the flow of viscous fluids through a capillary could be precisely measured employing high-pressure liquid chromatography systems (HPLC) using glycerol solutions of moderate viscosity as a mobile phase, and correlated to the dynamic (absolute) viscosity. The parameters allowing calculation of the viscosity of glycerol calibration standards as a function of temperature were established. The measurements were made with volumes as small as 10 μL, and the use of an autosampler permitted unattended analysis of a large number samples. The method appears to be particularly well suited for the development of viscous formulations of therapeutic, protein-based macromolecules, where the amount sample is typically limited and relatively wide ranges of conditions are considered in the optimization process. The utility of the methods was illustrated by application to the development of concentrated inactivated virus vaccines. Full article
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Review

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Open AccessReview Exhaled Breath Condensate for Proteomic Biomarker Discovery
Chromatography 2014, 1(3), 108-119; doi:10.3390/chromatography1030108
Received: 8 May 2014 / Revised: 20 June 2014 / Accepted: 24 June 2014 / Published: 2 July 2014
Cited by 2 | PDF Full-text (192 KB) | HTML Full-text | XML Full-text
Abstract
Exhaled breath condensate (EBC) has been established as a potential source of respiratory biomarkers. Compared to the numerous small molecules identified, the protein content of EBC has remained relatively unstudied due to the methodological and technical difficulties surrounding EBC analysis. In this review,
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Exhaled breath condensate (EBC) has been established as a potential source of respiratory biomarkers. Compared to the numerous small molecules identified, the protein content of EBC has remained relatively unstudied due to the methodological and technical difficulties surrounding EBC analysis. In this review, we discuss the proteins identified in EBC, by mass spectrometry, focusing on the significance of those proteins identified. We will also review the limitations surrounding mass spectral EBC protein analysis emphasizing recommendations to enhance EBC protein identifications by mass spectrometry. Finally, we will provide insight into the future directions of the EBC proteomics field. Full article

Other

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Open AccessTechnical Note High-Throughput Mass Spectrometry Applied to Structural Genomics
Chromatography 2014, 1(4), 159-175; doi:10.3390/chromatography1040159
Received: 1 July 2014 / Revised: 3 September 2014 / Accepted: 11 September 2014 / Published: 9 October 2014
PDF Full-text (1100 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Mass spectrometry (MS) remains under-utilized for the analysis of expressed proteins because it is inaccessible to the non-specialist, and sample-turnaround from service labs is slow. Here, we describe 3.5 min Liquid-Chromatography (LC)-MS and 16 min LC-MSMS methods which are tailored to validation and
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Mass spectrometry (MS) remains under-utilized for the analysis of expressed proteins because it is inaccessible to the non-specialist, and sample-turnaround from service labs is slow. Here, we describe 3.5 min Liquid-Chromatography (LC)-MS and 16 min LC-MSMS methods which are tailored to validation and characterization of recombinant proteins in a high throughput structural biology pipeline. We illustrate the type and scope of MS data typically obtained from a 96-well expression and purification test for both soluble and integral membrane proteins (IMPs), and describe their utility in the selection of constructs for scale-up structural work, leading to cost and efficiency savings. We propose that value of MS data lies in how quickly it becomes available and that this can fundamentally change the way in which it is used. Full article
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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: Analytical and preparative applications of mixed-mode chromatography
Authors:
Tsutomu Arakawa, Daisuke Ejima, Mark Feild, Janice Davis
Affiliation:
Alliance Protein Laboratories; Ajinomoto Co. Inc.; Ajinomoto Althea, Inc.
Abstract:
This review covers our experience with mixed-mode chromatography for analysis and purification of proteins. Mixed-mode resins are composed of multiple protein binding sites, thereby providing different binding mechanisms that do not occur in such single-mode resins as ion-exchange and hydrophobic interaction chromatography. Commonly-used mixed-mode resins contain ionic and hydrophobic groups and hence can bind protein by electrostatic and hydrophobic interactions. While such multiple binding mechanisms render protein binding stronger, they do often complicate elution of the bound protein, as it may require disrupting both electrostatic and hydrophobic interactions simultaneously. We will review binding and elution properties of mixed-mode chromatography using a few model proteins. A novel finding in application of mixed-mode chromatography is resolution of isoforms of a same protein, which will also be discussed.
Keywords:
mixed-mode chromatography, electrostatic, hydrophobic, isoform, elution, arginine.

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