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Membranes
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Membrane-Active Proteins/Peptides: Mechanism and Biomedical Applications
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Membrane-Active Proteins/Peptides: Mechanism and Biomedical Applications

A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Biological Membrane Functions".

Deadline for manuscript submissions: closed (31 May 2022) | Viewed by 10295

Special Issue Editor

Prof. Dr. Long-Sen Chang

E-Mail Website
Guest Editor
Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan
Interests: snake venom proteins; cellular signaling; pharmacogenomics; translational medicine

Special Issue Information

Dear Colleagues,

Many biologically active proteins and peptides exert their activity on the cell membrane.  The mechanism by which they act on the cell membrane may be to destroy the cell membrane, form a pore structure in the membrane, enter the cell to destroy the integrity of the organelle membrane structure, or trigger the cell signal transduction pathway by interfering with the cell membrane structure. These effects can be further applied to biomedical research or the development of biopharmaceutics to display antibacterial or anti-cancer effects.  In addition, the technology of protein engineering, chemical modification or formation of complexes with lipids can further enhance the biological activity of proteins and peptides on the membrane, and even convert non-biologically active proteins/peptides to actively interact with biological membranes.

This special issue will focus on the mechanism of protein/peptide-membrane interaction and its biomedical applications. It welcomes both original contributions and reviews in the following areas: (1) the mechanism of protein/peptide-membrane interaction; (2) the functional activities of protein/peptide-membrane interaction in cancer treatment; (3) the membrane-disrupting mechanism of antimicrobial protein/peptide; (4) the mechanism by which natural toxins destroy biological membranes; (5) The engineering of protein/peptide interaction with membrane/phospholipid; or (6) the interaction between protein/peptide and membrane induces cell signaling pathways.

Prof. Dr. Long-Sen Chang
Guest Editor

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. Membranes 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

  • Membrane-active proteins/peptides
  • Membrane-disruption mechanism
  • Membrane-perturbing mechanism
  • Biomedical applications
  • Cellular signaling pathway
  • Engineering of membrane-active proteins/peptides

Published Papers (4 papers)

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Research

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19 pages, 2908 KiB  
Article
Ceramide Phosphoethanolamine as a Possible Marker of Periodontal Disease
by Maja Grundner, Haris Munjaković, Tilen Tori, Kristina Sepčić, Rok Gašperšič, Čedomir Oblak, Katja Seme, Graziano Guella, Francesco Trenti and Matej Skočaj
Membranes 2022, 12(7), 655; https://doi.org/10.3390/membranes12070655 - 25 Jun 2022
Cited by 3 | Viewed by 2174
Abstract
Periodontal disease is a chronic oral inflammatory disorder initiated by pathobiontic bacteria found in dental plaques—complex biofilms on the tooth surface. The disease begins as an acute local inflammation of the gingival tissue (gingivitis) and can progress to periodontitis, which eventually leads to [...] Read more.
Periodontal disease is a chronic oral inflammatory disorder initiated by pathobiontic bacteria found in dental plaques—complex biofilms on the tooth surface. The disease begins as an acute local inflammation of the gingival tissue (gingivitis) and can progress to periodontitis, which eventually leads to the formation of periodontal pockets and ultimately results in tooth loss. The main problem in periodontology is that the diagnosis is based on the assessment of the already obvious tissue damage. Therefore, it is necessary to improve the current diagnostics used to assess periodontal disease. Using lipidomic analyses, we show that both crucial periodontal pathogens, Porphyromonas gingivalis and Tannerella forsythia, synthesize ceramide phosphoethanolamine (CPE) species, membrane sphingolipids not typically found in vertebrates. Previously, it was shown that this particular lipid can be specifically detected by an aegerolysin protein, erylysin A (EryA). Here, we show that EryA can specifically bind to CPE species from the total lipid extract from P. gingivalis. Furthermore, using a fluorescently labelled EryA-mCherry, we were able to detect CPE species in clinical samples of dental plaque from periodontal patients. These results demonstrate the potential of specific periodontal pathogen-derived lipids as biomarkers for periodontal disease and other chronic inflammatory diseases. Full article
(This article belongs to the Special Issue Membrane-Active Proteins/Peptides: Mechanism and Biomedical Applications)
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9 pages, 667 KiB  
Communication
Bio-Membrane Internalization Mechanisms of Arginine-Rich Cell-Penetrating Peptides in Various Species
by Betty Revon Liu, Shiow-Her Chiou, Yue-Wern Huang and Han-Jung Lee
Membranes 2022, 12(1), 88; https://doi.org/10.3390/membranes12010088 - 13 Jan 2022
Cited by 12 | Viewed by 2841
Abstract
Recently, membrane-active peptides or proteins that include antimicrobial peptides (AMPs), cytolytic proteins, and cell-penetrating peptides (CPPs) have attracted attention due to their potential applications in the biomedical field. Among them, CPPs have been regarded as a potent drug/molecules delivery system. Various cargoes, such [...] Read more.
Recently, membrane-active peptides or proteins that include antimicrobial peptides (AMPs), cytolytic proteins, and cell-penetrating peptides (CPPs) have attracted attention due to their potential applications in the biomedical field. Among them, CPPs have been regarded as a potent drug/molecules delivery system. Various cargoes, such as DNAs, RNAs, bioactive proteins/peptides, nanoparticles and drugs, can be carried by CPPs and delivered into cells in either covalent or noncovalent manners. Here, we focused on four arginine-rich CPPs and reviewed the mechanisms that these CPPs used for intracellular uptake across cellular plasma membranes. The varying transduction efficiencies of them alone or with cargoes were discussed, and the membrane permeability was also expounded for CPP/cargoes delivery in various species. Direct membrane translocation (penetration) and endocytosis are two principal mechanisms for arginine-rich CPPs mediated cargo delivery. Furthermore, the amino acid sequence is the primary key factor that determines the cellular internalization mechanism. Importantly, the non-cytotoxic nature and the wide applicability make CPPs a trending tool for cellular delivery. Full article
(This article belongs to the Special Issue Membrane-Active Proteins/Peptides: Mechanism and Biomedical Applications)
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12 pages, 2738 KiB  
Article
NMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations
by Minseon Kim, Jinyoung Son and Yongae Kim
Membranes 2021, 11(11), 799; https://doi.org/10.3390/membranes11110799 - 20 Oct 2021
Cited by 3 | Viewed by 1820
Abstract
Alzheimer’s disease (AD) is classified as an amyloid-related disease. Amyloid beta (Aβ) is a transmembrane protein known to play a major role in the pathogenesis of AD. These Aβ proteins can form ion channels or pores in the cell membrane. Studies have elucidated [...] Read more.
Alzheimer’s disease (AD) is classified as an amyloid-related disease. Amyloid beta (Aβ) is a transmembrane protein known to play a major role in the pathogenesis of AD. These Aβ proteins can form ion channels or pores in the cell membrane. Studies have elucidated the structure of the transmembrane domain of Aβ ion channels. In addition, various studies have investigated substances that block or inhibit the formation of Aβ ion channels. Zinc ions are considered as potential inhibitors of AD. In this study, we focused on the transmembrane domain and some external domains of the Aβ protein (hAPP-TM), and solution-state NMR was used to confirm the effect on residues of the protein in the presence of zinc ions. In addition, we sought to confirm the structure and orientation of the protein in the presence of the bicelle using solid-state NMR. Full article
(This article belongs to the Special Issue Membrane-Active Proteins/Peptides: Mechanism and Biomedical Applications)
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Review

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16 pages, 1211 KiB  
Review
Design of Membrane Active Peptides Considering Multi-Objective Optimization for Biomedical Application
by Niels Röckendorf, Christian Nehls and Thomas Gutsmann
Membranes 2022, 12(2), 180; https://doi.org/10.3390/membranes12020180 - 2 Feb 2022
Cited by 8 | Viewed by 2542
Abstract
A multitude of membrane active peptides exists that divides into subclasses, such as cell penetrating peptides (CPPs) capable to enter eukaryotic cells or antimicrobial peptides (AMPs) able to interact with prokaryotic cell envelops. Peptide membrane interactions arise from unique sequence motifs of the [...] Read more.
A multitude of membrane active peptides exists that divides into subclasses, such as cell penetrating peptides (CPPs) capable to enter eukaryotic cells or antimicrobial peptides (AMPs) able to interact with prokaryotic cell envelops. Peptide membrane interactions arise from unique sequence motifs of the peptides that account for particular physicochemical properties. Membrane active peptides are mainly cationic, often primary or secondary amphipathic, and they interact with membranes depending on the composition of the bilayer lipids. Sequences of these peptides consist of short 5–30 amino acid sections derived from natural proteins or synthetic sources. Membrane active peptides can be designed using computational methods or can be identified in screenings of combinatorial libraries. This review focuses on strategies that were successfully applied to the design and optimization of membrane active peptides with respect to the fact that diverse features of successful peptide candidates are prerequisites for biomedical application. Not only membrane activity but also degradation stability in biological environments, propensity to induce resistances, and advantageous toxicological properties are crucial parameters that have to be considered in attempts to design useful membrane active peptides. Reliable assay systems to access the different biological characteristics of numerous membrane active peptides are essential tools for multi-objective peptide optimization. Full article
(This article belongs to the Special Issue Membrane-Active Proteins/Peptides: Mechanism and Biomedical Applications)
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