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Molecules
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Separation and Purification of Peptides
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Separation and Purification of Peptides

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: closed (30 September 2021) | Viewed by 12762

Special Issue Editors

Dr. Martina Catani

E-Mail Website
Guest Editor
Department of Chemistry and Pharmaceutical Sciences, University of Ferrara, Ferrara, Italy
Interests: HPLC; preparative chromatography; continuous chromatography; therapeutic biomolecules; peptides; thermodynamics; kinetics
Dr. Eduardo Sommella

E-Mail Website
Guest Editor
Department of Pharmacy, University of Salerno, Fisciano, SA, Italy
Interests: liquid chromatography; peptides; metabolites; high-resolution mass spectrometry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue is focused on peptides, a unique class of biomolecules that is increasingly attracting interest in many fields of science.

Peptides have a fundamental role in the human body, being involved in many biological processes. For this reason, they are currently reputed to be ideal biomarkers for the diagnosis of many diseases, including neurodegenerative ones, cancer, and diabetes.

Moreover, the discovery of peptide hormone insulin in 1920 and its role in the treatment of diabetes has been considered one of the most important medical discoveries of the last century, which has paved the way to research into and identification of other therapeutic peptides. Currently, there are more than 100 approved peptide drugs, forming a novel class of biotherapeutics; however, the number of commercialized therapeutic peptides is expected to dramatically increase in the very near future.

For the reasons above, there is an increasing demand for highly efficient methods for the analysis of peptides. Moreover, since therapeutic peptides need to be produced in a large scale in pharma industries, there is also an urgent need for the development of purification methods able to isolate the target peptide with adequate purity for pharmaceutical scopes.

Liquid chromatography and related techniques have always been the preferred method of choice for both the analysis and purification of peptides. The number of scientific papers on this topic is growing year after year, and very recently, even a new term (“peptidomics”) has been established to recognize a systematic, comprehensive analysis of peptides in biological samples.

The aim of this Special Issue is to cover both fundamental and practical aspects of analysis and purification of peptides by means of liquid chromatography and related techniques. Researchers working in this field may contribute with either an original work or a review article. Manuscripts focused on fundamental aspects on retention of peptides, innovative methods for the purification, latest advancements on peptidomics, and analysis of peptides as biomarkers are particularly welcome.

Dr. Martina Catani
Dr. Eduardo Sommella
Guest Editors

Manuscript Submission Information

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. 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. Molecules is an international peer-reviewed open access semimonthly 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 2700 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

  • analysis of peptides
  • purification of peptides
  • liquid chromatography
  • liquid chromatography coupled to mass spectrometry
  • preparative chromatography
  • peptide biomarkers
  • peptidomics

Published Papers (4 papers)

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Research

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11 pages, 12870 KiB  
Article
Easy Expression and Purification of Fluorescent N-Terminal BCL11B CCHC Zinc Finger Domain
by Anne Susemihl, Felix Nagel, Piotr Grabarczyk, Christian A. Schmidt and Mihaela Delcea
Molecules 2021, 26(24), 7576; https://doi.org/10.3390/molecules26247576 - 14 Dec 2021
Cited by 3 | Viewed by 2622
Abstract
Zinc finger proteins play pivotal roles in health and disease and exert critical functions in various cellular processes. A majority of zinc finger proteins bind DNA and act as transcription factors. B-cell lymphoma/leukemia 11B (BCL11B) represents one member of the large family of [...] Read more.
Zinc finger proteins play pivotal roles in health and disease and exert critical functions in various cellular processes. A majority of zinc finger proteins bind DNA and act as transcription factors. B-cell lymphoma/leukemia 11B (BCL11B) represents one member of the large family of zinc finger proteins. The N-terminal domain of BCL11B was shown to be crucial for BCL11B to exert its proper function by homodimerization. Here, we describe an easy and fast preparation protocol to yield the fluorescently tagged protein of the recombinant N-terminal BCL11B zinc finger domain (BCL11B42-94) for in vitro studies. First, we expressed fluorescently tagged BCL11B42-94 in E. coli and described the subsequent purification utilizing immobilized metal ion affinity chromatography to achieve very high yields of a purified fusion protein of 200 mg/L culture. We proceeded with characterizing the atypical zinc finger domain using circular dichroism and size exclusion chromatography. Validation of the functional fluorescent pair CyPet-/EYFP-BCL11B42-94 was achieved with Förster resonance energy transfer. Our protocol can be utilized to study other zinc finger domains to expand the knowledge in this field. Full article
(This article belongs to the Special Issue Separation and Purification of Peptides)
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14 pages, 1513 KiB  
Article
High-Resolution Mass Spectrometry and Chemometrics for the Detailed Characterization of Short Endogenous Peptides in Milk By-Products
by Carmela Maria Montone, Sara Elsa Aita, Chiara Cavaliere, Andrea Cerrato, Aldo Laganà, Susy Piovesana and Anna Laura Capriotti
Molecules 2021, 26(21), 6472; https://doi.org/10.3390/molecules26216472 - 27 Oct 2021
Cited by 5 | Viewed by 1695
Abstract
The process of cheese-making has long been part of human food culture and nowadays dairy represents a large sector of the food industry. Being the main byproduct of cheese-making, the revalorization of milk whey is nowadays one of the primary goals in alignment [...] Read more.
The process of cheese-making has long been part of human food culture and nowadays dairy represents a large sector of the food industry. Being the main byproduct of cheese-making, the revalorization of milk whey is nowadays one of the primary goals in alignment with the principles of the circular economy. In the present paper, a deep and detailed investigation of short endogenous peptides in milk and its byproducts (whole whey, skimmed whey, and whey permeate) was carried out by high-resolution mass spectrometry, with a dedicated suspect screening data acquisition and data analysis approach. A total of 79 short peptides was tentatively identified, including several sequences already known for their exerted biological activities. An unsupervised chemometric approach was then employed for highlighting the differences in the short peptide content among the four sets of samples. Whole and skimmed whey showed not merely a higher content of short bioactive peptides compared to whole milk, but also a peculiar composition of peptides that are likely generated during the process of cheese-making. The results clearly demonstrate that whey represents a valuable source of bioactive compounds and that the set-up of processes of revalorization of milk byproducts is a promising path in the obtention of high revenue-generating products from dairy industrial waste. Full article
(This article belongs to the Special Issue Separation and Purification of Peptides)
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13 pages, 3046 KiB  
Article
Expanding the Use of Dynamic Electrostatic Repulsion Reversed-Phase Chromatography: An Effective Elution Mode for Peptides Control and Analysis
by Giulia Mazzoccanti, Simone Manetto, Michele Bassan, Marco Macis, Antonia Iazzetti, Walter Cabri, Antonio Ricci and Francesco Gasparrini
Molecules 2021, 26(14), 4348; https://doi.org/10.3390/molecules26144348 - 19 Jul 2021
Cited by 1 | Viewed by 2267
Abstract
Bioactive peptides are increasingly used in clinical practice. Reversed-phase chromatography using formic or trifluoroacetic acid in the mobile phase is the most widely used technique for their analytical control. However, sometimes it does not prove sufficient to solve challenging chromatographic problems. In the [...] Read more.
Bioactive peptides are increasingly used in clinical practice. Reversed-phase chromatography using formic or trifluoroacetic acid in the mobile phase is the most widely used technique for their analytical control. However, sometimes it does not prove sufficient to solve challenging chromatographic problems. In the search for alternative elution modes, the dynamic electrostatic repulsion reversed-phase was evaluated to separate eight probe peptides characterised by different molecular weights and isoelectric points. This technique, which involves TBAHSO4 in the mobile phase, provided the lowest asymmetry and peak width at half height values and the highest in peak capacity (about 200 for a gradient of 30 min) and resolution concerning the classic reversed-phase. All analyses were performed using cutting-edge columns developed for peptide separation, and the comparison of the chromatograms obtained shows how the dynamic electrostatic repulsion reversed-phase is an attractive alternative to the classic reversed-phase. Full article
(This article belongs to the Special Issue Separation and Purification of Peptides)
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Review

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20 pages, 690 KiB  
Review
Downstream Processing of Therapeutic Peptides by Means of Preparative Liquid Chromatography
by Chiara De Luca, Giulio Lievore, Desiree Bozza, Alessandro Buratti, Alberto Cavazzini, Antonio Ricci, Marco Macis, Walter Cabri, Simona Felletti and Martina Catani
Molecules 2021, 26(15), 4688; https://doi.org/10.3390/molecules26154688 - 03 Aug 2021
Cited by 26 | Viewed by 5319
Abstract
The market of biomolecules with therapeutic scopes, including peptides, is continuously expanding. The interest towards this class of pharmaceuticals is stimulated by the broad range of bioactivities that peptides can trigger in the human body. The main production methods to obtain peptides are [...] Read more.
The market of biomolecules with therapeutic scopes, including peptides, is continuously expanding. The interest towards this class of pharmaceuticals is stimulated by the broad range of bioactivities that peptides can trigger in the human body. The main production methods to obtain peptides are enzymatic hydrolysis, microbial fermentation, recombinant approach and, especially, chemical synthesis. None of these methods, however, produce exclusively the target product. Other species represent impurities that, for safety and pharmaceutical quality reasons, must be removed. The remarkable production volumes of peptide mixtures have generated a strong interest towards the purification procedures, particularly due to their relevant impact on the manufacturing costs. The purification method of choice is mainly preparative liquid chromatography, because of its flexibility, which allows one to choose case-by-case the experimental conditions that most suitably fit that particular purification problem. Different modes of chromatography that can cover almost every separation case are reviewed in this article. Additionally, an outlook to a very recent continuous chromatographic process (namely Multicolumn Countercurrent Solvent Gradient Purification, MCSGP) and future perspectives regarding purification strategies will be considered at the end of this review. Full article
(This article belongs to the Special Issue Separation and Purification of Peptides)
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