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Peptides and Their Derivatives as Chemical Sensors

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A special issue of Chemosensors (ISSN 2227-9040). This special issue belongs to the section "Materials for Chemical Sensing".

Deadline for manuscript submissions: closed (20 March 2022) | Viewed by 12527

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Special Issue Editors

Dr. Krzysztof Żamojć

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Guest Editor

Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland
Interests: fluorescence spectroscopy; fluorescence quenching; sensors of reactive oxygen and nitrogen species; peptide–metal complexes

Dr. Joanna Makowska

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Guest Editor

Faculty of Chemistry, University of Gdańsk, Wita Stwosza63, 80-308 Gdańsk, Poland
Interests: biophysical characterization of peptide–small systems interactions; thermal stability of peptides and proteins in solution (microcalorimetry, VP-DSC); coordination properties of peptides; molecular dynamics simulations; potentiometric method

Dr. Dariusz Wyrzykowski

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Guest Editor

Faculty of Chemistry, University of Gdańsk, Wita Stwosza63, 80-308 Gdańsk, Poland
Interests: isothermal titration calorimetry; potentiometric and conductometric methods; ligand–macromolecule interactions; coordination chemistry

Special Issue Information

Dear Colleagues,

It is a great pleasure for us to invite you to a Special Issue of Chemosensors concerning the utilization of peptides and their derivatives in all aspects of sensing. The development of new molecular sensors with peptidic receptors for a variety of analytes (among others, metal ions, enzymes, drugs, and low-molecular-weight compounds of biological relevance) has already attracted increasing interest, mainly due to their many advantages and applications. According to that, chemical indicators based on synthetic peptides have received increasing attention as a great alternative to protein-based sensors—they can be synthesized chemically, are stable, can be easily modified, and very often exhibit strong binding properties. Furthermore, peptides can functionally bind to environmentally sensitive dyes or other organic agents in biological contexts, suggesting tools for in vivo imaging and analysis.

We would like to invite scientists to participate through the submission of research articles, (mini)reviews, communications or opinions, focusing on the use of peptides and their derivatives in the field of sensing. The main goal and the scope of this Special Issue is to present recent advances in the application of that unique class of compounds in bio- and chemical target sensing in a variety of systems and with the use of various techniques. The methods for selective detection of peptides are also welcome.

Dr. Krzysztof Żamojć
Dr. Joanna Makowska
Dr. Dariusz Wyrzykowski
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. Chemosensors 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 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

peptides and their derivatives
chemical sensing
biosensing

Published Papers (5 papers)

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Research

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14 pages, 1375 KiB

Open AccessArticle

A Peptide-Based Trap for Metal Ions Studied by Electron Paramagnetic Resonance

by Victoria N. Syryamina, Alvaro S. Siano, Fernando Formaggio and Marta De Zotti

Chemosensors 2022, 10(2), 71; https://0-doi-org.brum.beds.ac.uk/10.3390/chemosensors10020071 - 10 Feb 2022

Viewed by 2112

Abstract

Peptide-based materials provide a versatile platform for sensing and ion sequestration since peptides are endowed with stimuli-responsive properties. The mechanism of molecular sensing is often based on peptide structural changes (or switching), caused by the binding of the target molecule. One scope of sensing applications is the selection of a specific analyte, which may be achieved by adjusting the structure of the peptide binding site. Therefore, exact knowledge of peptide properties and 3D-structure in the ‘switched’ state is desirable for tuning the detection and for further molecular construction. Hence, here we demonstrate the performance of Electron Paramagnetic Resonance (EPR) spectroscopy in the identification of metal ion binding by the antimicrobial peptide trichogin GA IV. Na(I), Ca(II), and Cu(II) ions were probed as analytes to evaluate the impact of coordination number, ionic radii, and charge. Conclusions drawn by EPR are in line with literature data, where other spectroscopic techniques were exploited to study peptide-ion interactions for trichogin GA IV, and the structural switch from an extended helix to a hairpin structure, wrapped around the metal ion upon binding of divalent cations was proposed. Full article

(This article belongs to the Special Issue Peptides and Their Derivatives as Chemical Sensors)

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12 pages, 3604 KiB

Open AccessArticle

Peptide Linked Diacetylene Amphiphiles for Detection of Epitope Specific Antibodies

by Natalie Tran, Priyanka Shiveshwarkar and Justyn Jaworski

Chemosensors 2022, 10(2), 62; https://0-doi-org.brum.beds.ac.uk/10.3390/chemosensors10020062 - 03 Feb 2022

Cited by 1 | Viewed by 2011

Abstract

Antibodies produced in response to adaptive immunity provide a receptor with multiple sites for binding to a distinct epitope of an antigen. Determining antibody levels to specific antigens has important clinical applications in assessing immune status or deficiency, monitoring infectious or autoimmune diseases, and diagnosing allergies. Leveraging that a specific antibody will bind to a distinct small peptide epitope without requiring the entire antigen to be present, we demonstrate in this work a proof-of-concept assay to detect the presence of an antibody by using peptide epitopes linked to an amphiphile to generate a vesicle-based sensing system. By affording multiple copies of the epitope site on the vesicle, we revealed that the vesicles visibly aggregate in response to an antibody specific for that epitope due to multivalent binding provided by the antibody. We also uncovered the role of peptide surface density in providing accessible epitopes on the vesicles for antibody binding. In summary, using a peptide derived from the coat protein of human influenza virus directly linked to a diacetylene-containing amphiphile afforded peptide-laden vesicles that proved capable of detecting the presence of antibodies specific for human influenza hemagglutinin. Full article

(This article belongs to the Special Issue Peptides and Their Derivatives as Chemical Sensors)

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Graphical abstract

17 pages, 1941 KiB

Open AccessArticle

Fluorescent Analogues of FRH Peptide: Cu(II) Binding and Interactions with ds-DNA/RNA

by Marta Košćak, Ivona Krošl, Biserka Žinić and Ivo Piantanida

Chemosensors 2022, 10(1), 34; https://0-doi-org.brum.beds.ac.uk/10.3390/chemosensors10010034 - 14 Jan 2022

Cited by 5 | Viewed by 2407

Abstract

Four novel peptidoids, derived from the Phe-Arg-His (FRH) peptide motif, were prepared by replacing the histidine heterocycle with triazole and consequent triazole-fluorophore (coumarin) extension and also replacing arginine with less voluminous lysine. So the constructed Phe-Lys-Ala(triazole) (FKA(triazole)) peptidoids bind Cu²⁺ cations in water with a strong, nanomolar affinity comparable to the parent FRH and its known analogs, demonstrating that triazole can coordinate copper similarly as histidine. Moreover, even short KA(triazole)coumarin showed submicromolar affinity to Cu²⁺. Only FKA(triazole)coumarin with free amino groups and its shorter analog KA(triazole)coumarin showed strong induced CD spectra upon Cu²⁺ cation binding. Thus, KA(triazole)coumarin can be considered as the shortest peptidoid sequence with highly sensitive fluorescent and chiral CD response for Cu²⁺ cation, encouraging further studies with other metal cations. The FKA(triazole) coumarin peptidoids show biorelevant, 10 µM affinity to ds-DNA and ds-RNA, binding within DNA/RNA grooves. Intriguingly, only peptidoid complexes with Cu²⁺ strongly stabilize ds-DNA and ds-RNA against thermal denaturation, suggesting significant interactions of Cu²⁺ cation within the DNA/RNA binding site. Full article

(This article belongs to the Special Issue Peptides and Their Derivatives as Chemical Sensors)

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15 pages, 3507 KiB

Open AccessArticle

Sensors to the Diagnostic Assessment of Anticancer and Antimicrobial Therapies Effectiveness by Drugs a with Pyrazine Scaffold

by Marta Domżalska, Aleksandra M. Dąbrowska, Dawid Chojnowski, Mariusz Makowski and Agnieszka Chylewska

Chemosensors 2022, 10(1), 24; https://0-doi-org.brum.beds.ac.uk/10.3390/chemosensors10010024 - 07 Jan 2022

Cited by 2 | Viewed by 2124

Abstract

Treatment with pyrazine derivatives—antituberculosis pyrazinamide (PZA), anticancer bortezomib (BZM), and antifungal pyrazine-2-amidoxime (PAOX) and pyrazine-2-thiocarboxamide (PTCA)—is associated with side effects, as observed in the case of other therapeutic drugs. To prevent the side effects of pyrazine derivatives, researchers are working to develop a universal method that will detect these compounds in body fluids. There is a lack of literature data about voltammetric measurements with poly-L-amino acid-modified GCEs surfaces. The available reports describe the application of various modifications of these electrodes for the detection of different active substances of drugs; however, they do not indicate one particular method for the detection of drugs with a pyrazine skeleton. This research aimed to prepare three types of glassy carbon electrodes (GCEs) with modified surfaces by electropolymerization using 1, 10, and 100 mM solutions of L-glycine (Gly), L-alanine (Ala), L-lysine (Lys), respectively. The poly-amino acid coatings applied on GCE surfaces were analyzed in detail under a three-dimensional (3D) microscope and were used as chemosensors of four pyrazine drugs in stoichiometric tests. The results were compared with the measurements made on an unmodified GCE. To obtain reliable results, the linearity of measurements was also verified in the concentration gradient and appropriate scanning speed was chosen to achieve the most accurate measurements. Full article

(This article belongs to the Special Issue Peptides and Their Derivatives as Chemical Sensors)

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Review

Jump to: Research

26 pages, 1197 KiB

Open AccessReview

Veni, Vidi, Vici: Immobilized Peptide-Based Conjugates as Tools for Capture, Analysis, and Transformation

by Marta Kowalska, Dominik Popiel, Martyna Walter, Remigiusz Bąchor, Monika Biernat, Marek Cebrat, Monika Kijewska, Mariola Kuczer, Maciej Modzel and Alicja Kluczyk

Chemosensors 2022, 10(1), 31; https://0-doi-org.brum.beds.ac.uk/10.3390/chemosensors10010031 - 12 Jan 2022

Cited by 4 | Viewed by 3173

Abstract

Analysis of peptide biomarkers of pathological states of the organism is often a serious challenge, due to a very complex composition of the cell and insufficient sensitivity of the current analytical methods (including mass spectrometry). One of the possible ways to overcome this problem is sample enrichment by capturing the selected components using a specific solid support. Another option is increasing the detectability of the desired compound by its selective tagging. Appropriately modified and immobilized peptides can be used for these purposes. In addition, they find application in studying the specificity and activity of proteolytic enzymes. Immobilized heterocyclic peptide conjugates may serve as metal ligands, to form complexes used as catalysts or analytical markers. In this review, we describe various applications of immobilized peptides, including selective capturing of cysteine-containing peptides, tagging of the carbonyl compounds to increase the sensitivity of their detection, enrichment of biological samples in deoxyfructosylated peptides, and fishing out of tyrosine–containing peptides by the formation of azo bond. Moreover, the use of the one-bead-one-compound peptide library for the analysis of substrate specificity and activity of caspases is described. Furthermore, the evolution of immobilization from the solid support used in peptide synthesis to nanocarriers is presented. Taken together, the examples presented here demonstrate immobilized peptides as a multifunctional tool, which can be successfully used to solve multiple analytical problems. Full article

(This article belongs to the Special Issue Peptides and Their Derivatives as Chemical Sensors)

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