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Separations
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Peptide Synthesis, Separation and Purification
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Peptide Synthesis, Separation and Purification

A special issue of Separations (ISSN 2297-8739). This special issue belongs to the section "Chromatographic Separations".

Deadline for manuscript submissions: 10 August 2024 | Viewed by 1891

Special Issue Editor

Dr. Othman Al Musaimi

E-Mail Website
Guest Editor
1. School of Pharmacy, Faculty of Medical Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK
2. Department of Chemical Engineering, Imperial College London, London SW7 AZ, UK
Interests: peptide synthesis; separation; purification and greening
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Synthetic peptide manufacturing is substantially more expensive than small molecule manufacturing. Additionally, the larger the API molecule becomes, efficient purification and isolation becomes increasingly more important as well. The demand particularly increases as production quantities from tens to thousands of kilograms per year.

Given this context, this Special Issue of Separations, ‘Peptide Synthesis, Separation and Purification,’ invites scholars to submit their original research and review articles, covering various aspects of peptides purification including the synthetic approaches, separation methodologies, and the influence of hydrophobicity and solubility on the overall separation and purification behavior. Furthermore, we welcome papers addressing novel synthetic strategies that can deliver purer peptides and decrease the purification burden, as well as papers that incorporate computational, modeling, and machine learning approaches as these are powerful tools that can save time, cost, and effort.

Dr. Othman Al Musaimi
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at mdpi.longhoe.net 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. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short 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 thoroughly refereed through a single-blind 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 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 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • hydrophobicity
  • retention time prediction
  • solubility
  • retention behavior
  • peptide separation
  • purification
  • denaturation

Published Papers (2 papers)

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Research

18 pages, 929 KiB  
Article
Improved Expression of Aggregation-Prone Tau Proteins Using a Spidroin-Derived Solubility Tag
by Kevin Muwonge, Bedri Yaman, Attila Mészáros, Giorgio Russo, Alexander Volkov and Peter Tompa
Separations 2024, 11(7), 198; https://doi.org/10.3390/separations11070198 - 25 Jun 2024
Viewed by 818
Abstract
Tauopathies, a group of neurodegenerative disorders, are characterized by the abnormal aggregation of microtubule-associated Tau proteins in neurons and glial cells. The process of Tau proteins transitioning from soluble, intrinsically disordered monomers to disease-associated aggregates is still unclear. Investigating these molecular mechanisms requires [...] Read more.
Tauopathies, a group of neurodegenerative disorders, are characterized by the abnormal aggregation of microtubule-associated Tau proteins in neurons and glial cells. The process of Tau proteins transitioning from soluble, intrinsically disordered monomers to disease-associated aggregates is still unclear. Investigating these molecular mechanisms requires the reconstitution of such processes in cellular and in vitro models using recombinant proteins at high purity and yield. However, the production of phase-separating or aggregation-prone recombinant proteins like Tau’s hydrophobic-rich domains or disease mutation-carrying variants on a large scale is highly challenging due to their limited solubility. To overcome this challenge, we have developed an improved strategy for expressing and purifying recombinant Tau proteins using the major ampullate spidroin-derived solubility tag (MaSp-NT*). This approach involves using NT* as a fusion tag to enhance the solubility and stability of expressed proteins by forming micelle-like particles within the cytosol of E. coli cells. We found that fusion with the NT* tag significantly increased the solubility and yield of highly hydrophobic and/or aggregation-prone Tau constructs. Our purification method for NT* fusion proteins yielded up to twenty-fold higher amounts than proteins purified using our novel tandem-tag (6xHis-SUMO-Tau-Heparin) purification system. This enhanced expression and yield were demonstrated with full-length Tau (hT40/Tau441), its particularly aggregation-prone repeat domain (Tau-MTBR), and Frontotemporal dementia (FTD)-associated mutant (Tau-P301L). These advancements offer promising avenues for the production of large quantities of Tau proteins suitable for in vitro experimental techniques such as nuclear magnetic resonance (NMR) spectroscopy without the need for a boiling step, bringing us closer to effective treatments for tauopathies. Full article
(This article belongs to the Special Issue Peptide Synthesis, Separation and Purification)
18 pages, 3129 KiB  
Article
Efficient Quality Control of Peptide Pools by UHPLC and Simultaneous UV and HRMS Detection
by Gaby Bosc-Bierne, Shireen Ewald, Oliver J. Kreuzer and Michael G. Weller
Separations 2024, 11(5), 156; https://doi.org/10.3390/separations11050156 - 16 May 2024
Viewed by 735
Abstract
Peptide pools consist of short amino acid sequences and have proven to be versatile tools in various research areas in immunology and clinical applications. They are commercially available in many different compositions and variants. However, unlike other reagents that consist of only one [...] Read more.
Peptide pools consist of short amino acid sequences and have proven to be versatile tools in various research areas in immunology and clinical applications. They are commercially available in many different compositions and variants. However, unlike other reagents that consist of only one or a few compounds, peptide pools are highly complex products which makes their quality control a major challenge. Quantitative peptide analysis usually requires sophisticated methods, in most cases isotope-labeled standards and reference materials. Usually, this would be prohibitively laborious and expensive. Therefore, an approach is needed to provide a practical and feasible method for quality control of peptide pools. With insufficient quality control, the use of such products could lead to incorrect experimental results, worsening the well-known reproducibility crisis in the biomedical sciences. Here we propose the use of ultra-high performance liquid chromatography (UHPLC) with two detectors, a standard UV detector at 214 nm for quantitative analysis and a high-resolution mass spectrometer (HRMS) for identity confirmation. To be cost-efficient and fast, quantification and identification are performed in one chromatographic run. An optimized protocol is shown, and different peak integration methods are compared and discussed. This work was performed using a peptide pool known as CEF advanced, which consists of 32 peptides derived from cytomegalovirus (CMV), Epstein–Barr virus (EBV) and influenza virus, ranging from 8 to 12 amino acids in length. Full article
(This article belongs to the Special Issue Peptide Synthesis, Separation and Purification)
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