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Membrane–Peptide Interactions: From Basics to Current Applications 2.0
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Membrane–Peptide Interactions: From Basics to Current Applications 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: closed (20 July 2022) | Viewed by 12537

Special Issue Editors

Prof. Dr. Nuno C. Santos

E-Mail Website
Guest Editor
Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisbon, Portugal
Interests: dengue virus; Zika virus; West Nile virus; HIV; viral entry inhibitors; broad-spectrum antivirals; antimicrobial peptides; antiviral peptides; biophysics; nanomedicine
Special Issues, Collections and Topics in MDPI journals
Dr. Sónia Gonçalves

E-Mail Website
Guest Editor
Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisbon, Portugal
Interests: antimicrobial peptides; antimicrobial biomaterials
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Natural and synthetic membrane active peptides have been gaining increasing interest during the last decades. Their attractiveness for researchers relies, among other factors, on their biological role in host defense and their wide potential in multiple disciplines, with a special focus on the medical field. Understanding the determinants for peptide–membrane interactions may enhance the knowledge of biomembrane functions such as membrane transport, fusion, and signaling processes, and it may bring some light on potential applications of peptides, as well as improve their design, contributing to the development of new agents for highly relevant applications, ranging from disease treatment to agricultural use.

Some key questions regarding peptide–membrane interactions remain to be answered. To address this question, the integration of multilateral approaches has been necessary, including biological, physical, and chemical approaches. This Special Issue aims to cover recent scientific contributions to the interaction of different types of peptide obtained from different sources (e.g., plants, animals, and fungus, as well as in silico designed) with cell membranes, as well as review articles addressing the current advances and state-of-the-art in this multidisciplinary field.

Potential topics include but are not limited to the following:

  • Peptide structure and function;
  • Antimicrobial peptides, anticancer peptides, cell-penetrating peptides, glycopeptides, cyclic peptides, and synthetic peptides;
  • Peptide formulations and their delivery;
  • Basic determinants for peptide–membrane interactions;
  • Peptide–membrane interactions in health and disease;
  • Therapeutic and biotech applications;
  • Computational modeling.
Dr. Nuno C. Santos
Dr. Sónia Gonçalves
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • Bioactive peptides
  • Therapeutics
  • Computational modeling
  • Peptide–membrane interactions
  • Lipid vesicles
  • Membrane models
  • Membrane probes
  • Drug delivery
  • Spectroscopy
  • Microscopy

Related Special Issue

Published Papers (6 papers)

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Editorial

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3 pages, 202 KiB  
Editorial
Membrane–Peptide Interactions: From Basics to Current Applications 2.0
by Sónia Gonçalves and Nuno C. Santos
Int. J. Mol. Sci. 2023, 24(8), 7202; https://doi.org/10.3390/ijms24087202 - 13 Apr 2023
Viewed by 802
Abstract
The interaction between peptides and biological membranes is of fundamental importance in the mechanism of numerous membrane-mediated cellular processes, including antimicrobial peptide action, hormone–receptor interactions, drug bioavailability across the blood–brain barrier, and viral fusion processes [...] Full article
(This article belongs to the Special Issue Membrane–Peptide Interactions: From Basics to Current Applications 2.0)

Research

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29 pages, 3805 KiB  
Article
The Antimicrobial Peptide 1018-K6 Interacts Distinctly with Eukaryotic and Bacterial Membranes, the Basis of Its Specificity and Bactericidal Activity
by Rosa Luisa Ambrosio, Catalina Ana Rosselló, Doralicia Casares, Gianna Palmieri, Aniello Anastasio and Pablo V. Escribá
Int. J. Mol. Sci. 2022, 23(20), 12392; https://doi.org/10.3390/ijms232012392 - 16 Oct 2022
Cited by 7 | Viewed by 1850
Abstract
Since penicillin was discovered, antibiotics have been critical in the fight against infections. However, antibiotic misuse has led to drug resistance, which now constitutes a serious health problem. In this context, antimicrobial peptides (AMPs) constitute a natural group of short proteins, varying in [...] Read more.
Since penicillin was discovered, antibiotics have been critical in the fight against infections. However, antibiotic misuse has led to drug resistance, which now constitutes a serious health problem. In this context, antimicrobial peptides (AMPs) constitute a natural group of short proteins, varying in structure and length, that act against certain types of bacterial pathogens. The antimicrobial peptide 1018-K6 (VRLIVKVRIWRR- NH2) has significant bactericidal and antibiofilm activity against Listeria monocytogenes isolates, and against different strains and serotypes of Salmonella. Here, the mechanism of action of 1018-K6 was explored further to understand the peptide–membrane interactions relevant to its activity, and to define their determinants. We combined studies with model synthetic membranes (liposomes) and model biological membranes, assessing the absorption maximum and the quenching of 1018-K6 fluorescence in aqueous and lipid environments, the self-quenching of carboxyfluorescein, as well as performing lipid sedimentation assays. The data obtained reflect the differential interactions of the 1018-K6 peptide with eukaryotic and prokaryotic membranes, and the specific interactions and mechanisms of action in the three prokaryotic species studied: Salmonella Typhimurium2GN, Escherichia coli3GN, and Staphylococcus aureus3GP. The AMP 1018-K6 is a candidate to prevent (food preservation) or treat (antibiotic use) infections caused by certain pathogenic bacteria, especially some that are resistant to current antibiotics. Full article
(This article belongs to the Special Issue Membrane–Peptide Interactions: From Basics to Current Applications 2.0)
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21 pages, 27090 KiB  
Article
Synergistic Action of Antimicrobial Lung Proteins against Klebsiella pneumoniae
by Víctor Fraile-Ágreda, Olga Cañadas, Timothy E. Weaver and Cristina Casals
Int. J. Mol. Sci. 2021, 22(20), 11146; https://doi.org/10.3390/ijms222011146 - 15 Oct 2021
Cited by 8 | Viewed by 2114
Abstract
As key components of innate immunity, lung antimicrobial proteins play a critical role in warding off invading respiratory pathogens. Lung surfactant protein A (SP-A) exerts synergistic antimicrobial activity with the N-terminal segment of the SP-B proprotein (SP-BN) against Klebsiella pneumoniae [...] Read more.
As key components of innate immunity, lung antimicrobial proteins play a critical role in warding off invading respiratory pathogens. Lung surfactant protein A (SP-A) exerts synergistic antimicrobial activity with the N-terminal segment of the SP-B proprotein (SP-BN) against Klebsiella pneumoniae K2 in vivo. However, the factors that govern SP-A/SP-BN antimicrobial activity are still unclear. The aim of this study was to identify the mechanisms by which SP-A and SP-BN act synergistically against K. pneumoniae, which is resistant to either protein alone. The effect of these proteins on K. pneumoniae was studied by membrane permeabilization and depolarization assays and transmission electron microscopy. Their effects on model membranes of the outer and inner bacterial membranes were analyzed by differential scanning calorimetry and membrane leakage assays. Our results indicate that the SP-A/SP-BN complex alters the ultrastructure of K. pneumoniae by binding to lipopolysaccharide molecules present in the outer membrane, forming packing defects in the membrane that may favor the translocation of both proteins to the periplasmic space. The SP-A/SP-BN complex depolarized and permeabilized the inner membrane, perhaps through the induction of toroidal pores. We conclude that the synergistic antimicrobial activity of SP-A/SP-BN is based on the capability of this complex, but not either protein alone, to alter the integrity of bacterial membranes. Full article
(This article belongs to the Special Issue Membrane–Peptide Interactions: From Basics to Current Applications 2.0)
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13 pages, 1895 KiB  
Article
Structural Water Stabilizes Protein Motifs in Liquid Protein Phase: The Folding Mechanism of Short β-Sheets Coupled to Phase Transition
by Dóra Papp, Imola Csilla Szigyártó, Bengt Nordén, András Perczel and Tamás Beke-Somfai
Int. J. Mol. Sci. 2021, 22(16), 8595; https://doi.org/10.3390/ijms22168595 - 10 Aug 2021
Cited by 3 | Viewed by 1667
Abstract
Macromolecular associates, such as membraneless organelles or lipid-protein assemblies, provide a hydrophobic environment, i.e., a liquid protein phase (LP), where folding preferences can be drastically altered. LP as well as the associated phase change from water (W) is an intriguing phenomenon related to [...] Read more.
Macromolecular associates, such as membraneless organelles or lipid-protein assemblies, provide a hydrophobic environment, i.e., a liquid protein phase (LP), where folding preferences can be drastically altered. LP as well as the associated phase change from water (W) is an intriguing phenomenon related to numerous biological processes and also possesses potential in nanotechnological applications. However, the energetic effects of a hydrophobic yet water-containing environment on protein folding are poorly understood. Here, we focus on small β-sheets, the key motifs of proteins, undergoing structural changes in liquid–liquid phase separation (LLPS) and also model the mechanism of energy-coupled unfolding, e.g., in proteases, during W → LP transition. Due to the importance of the accurate description for hydrogen bonding patterns, the employed models were studied by using quantum mechanical calculations. The results demonstrate that unfolding is energetically less favored in LP by ~0.3–0.5 kcal·mol−1 per residue in which the difference further increased by the presence of explicit structural water molecules, where the folded state was preferred by ~1.2–2.3 kcal·mol−1 per residue relative to that in W. Energetics at the LP/W interfaces was also addressed by theoretical isodesmic reactions. While the models predict folded state preference in LP, the unfolding from LP to W renders the process highly favorable since the unfolded end state has >1 kcal·mol−1 per residue excess stabilization. Full article
(This article belongs to the Special Issue Membrane–Peptide Interactions: From Basics to Current Applications 2.0)
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22 pages, 35950 KiB  
Article
Lipidation of Temporin-1CEb Derivatives as a Tool for Activity Improvement, Pros and Cons of the Approach
by Paulina Kosikowska-Adamus, Emilia Sikorska, Dariusz Wyrzykowski, Aleksandra Walewska, Anna Golda, Milena Deptuła, Michał Obuchowski, Adam Prahl, Michał Pikuła and Adam Lesner
Int. J. Mol. Sci. 2021, 22(13), 6679; https://doi.org/10.3390/ijms22136679 - 22 Jun 2021
Cited by 2 | Viewed by 1955
Abstract
The alarming raise of multi-drug resistance among human microbial pathogens makes the development of novel therapeutics a priority task. In contrast to conventional antibiotics, antimicrobial peptides (AMPs), besides evoking a broad spectrum of activity against microorganisms, could offer additional benefits, such as the [...] Read more.
The alarming raise of multi-drug resistance among human microbial pathogens makes the development of novel therapeutics a priority task. In contrast to conventional antibiotics, antimicrobial peptides (AMPs), besides evoking a broad spectrum of activity against microorganisms, could offer additional benefits, such as the ability to neutralize toxins, modulate inflammatory response, eradicate bacterial and fungal biofilms or prevent their development. The latter properties are of special interest, as most antibiotics available on the market have limited ability to diffuse through rigid structures of biofilms. Lipidation of AMPs is considered as an effective approach for enhancement of their antimicrobial potential and in vivo stability; however, it could also have undesired impact on selectivity, solubility or the aggregation state of the modified peptides. In the present work, we describe the results of structural modifications of compounds designed based on cationic antimicrobial peptides DK5 and CAR-PEG-DK5, derivatized at their N-terminal part with fatty acids with different lengths of carbon chain. The proposed modifications substantially improved antimicrobial properties of the final compounds and their effectiveness in inhibition of biofilm development as well as eradication of pre-formed 24 h old biofilms of Candida albicans and Staphylococcus aureus. The most active compounds (C5-DK5, C12-DK5 and C12-CAR-PEG-DK5) were also potent against multi-drug resistant Staphylococcus aureus USA300 strain and clinical isolates of Pseudomonas aeruginosa. Both experimental and in silico methods revealed strong correlation between the length of fatty acid attached to the peptides and their final membranolytic properties, tendency to self-assemble and cytotoxicity. Full article
(This article belongs to the Special Issue Membrane–Peptide Interactions: From Basics to Current Applications 2.0)
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15 pages, 7218 KiB  
Article
Antibiofilm Activity on Candida albicans and Mechanism of Action on Biomembrane Models of the Antimicrobial Peptide Ctn[15–34]
by Francisca Lidiane Linhares de Aguiar, Nuno C. Santos, Carolina Sidrim de Paula Cavalcante, David Andreu, Gandhi Radis Baptista and Sónia Gonçalves
Int. J. Mol. Sci. 2020, 21(21), 8339; https://doi.org/10.3390/ijms21218339 - 06 Nov 2020
Cited by 29 | Viewed by 3191
Abstract
Ctn[15–34], the C-terminal fragment of crotalicidin, an antimicrobial peptide from the South American rattlesnake Crotalus durissus terrificus venom, displays remarkable anti-infective and anti-proliferative activities. Herein, its activity on Candida albicans biofilms and its interaction with the cytoplasmic membrane of the fungal cell and [...] Read more.
Ctn[15–34], the C-terminal fragment of crotalicidin, an antimicrobial peptide from the South American rattlesnake Crotalus durissus terrificus venom, displays remarkable anti-infective and anti-proliferative activities. Herein, its activity on Candida albicans biofilms and its interaction with the cytoplasmic membrane of the fungal cell and with a biomembrane model in vitro was investigated. A standard C. albicans strain and a fluconazole-resistant clinical isolate were exposed to the peptide at its minimum inhibitory concentration (MIC) (10 µM) and up to 100 × MIC to inhibit biofilm formation and its eradication. A viability test using XTT and fluorescent dyes, confocal laser scanning microscopy, and atomic force microscopy (AFM) were used to observe the antibiofilm effect. To evaluate the importance of membrane composition on Ctn[15–34] activity, C. albicans protoplasts were also tested. Fluorescence assays using di-8-ANEPPS, dynamic light scattering, and zeta potential measurements using liposomes, protoplasts, and C. albicans cells indicated a direct mechanism of action that was dependent on membrane interaction and disruption. Overall, Ctn[15–34] showed to be an effective antifungal peptide, displaying antibiofilm activity and, importantly, interacting with and disrupting fungal plasma membrane. Full article
(This article belongs to the Special Issue Membrane–Peptide Interactions: From Basics to Current Applications 2.0)
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