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Synergy of Proteins, Peptides and Lipid Membranes in Vital Cellular Processes

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

Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 7535

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Special Issue Editors

Dr. Oleg V. Batishchev

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Guest Editor

Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, Russia
Interests: biophysics of cell and artificial membranes; bioelectrochemistry; physical chemistry of lipids; protein adsorption; self-assembly of complex protein structures; enveloped viruses; electroporation of lipid membranes; antimicrobial peptides; atomic force microscopy; fluorescent microscopy
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Dr. Sergey A. Akimov

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Guest Editor

Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, Russia
Interests: lipid membrane; theory of elasticity; membrane fusion; membrane fission; phase equilibrium; lipid domain; peptide; ion channel; pore; diffusion

Special Issue Information

Dear Colleagues,

In membrane biophysics, we commonly focus on the activity of specific proteins responsible for various functions in cells. However, the lipid component of cellular membranes sometimes plays a decisive role in processes, which are connected with membrane rearrangements during fusion, fission, tubulation, and pore formation in biological membranes. Specific features of membrane lipids may stimulate protein clustering and signal transduction. Thus, membrane biophysics concerns the synergy of proteins, peptides, and the lipid matrix, which together orchestrate vital cellular processes.

The aim of this Special issue is to highlight the role of interactions between different components of cellular membranes in regulating cell metabolism. We plan to specifically focus on the role of membrane elastic properties in protein organization and signal transductions, as well as to give new insights into sophisticated and sometimes surprising methods of protein–lipid interactions in membrane biophysics.

In this Special Issue, original research articles and reviews are welcome. Research areas may include (but are not limited to) the following:

The regulation of protein/peptide function by membrane elasticity;
Protein–lipid clustering into nanodomains, and the role of lipid composition in protein clustering and signal transduction across the cell membrane;
The clustering of water-soluble proteins triggered by the interaction with a lipid membrane;
Pore formation in lipid membranes by various peptides and proteins;
Protein-induced topological rearrangements of cellular membranes;
Membrane fusion and fission.

Dr. Oleg V. Batishchev
Dr. Sergey A. Akimov
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. 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

protein–lipid interactions
interfacial phenomena
raft
protein–lipid domain
protein clustering
lateral phase separation
theory of elasticity
pore formation
membrane-active peptide
membrane remodeling
mechanosensitivity

Published Papers (5 papers)

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Research

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14 pages, 3499 KiB

Open AccessArticle

The Membrane-Mediated Interaction of Liquid-Ordered Lipid Domains in the Presence of Amphipathic Peptides

by Konstantin V. Pinigin and Sergey A. Akimov

Membranes 2023, 13(10), 816; https://doi.org/10.3390/membranes13100816 - 28 Sep 2023

Viewed by 1029

Abstract

The lipid membranes of living cells are composed of a large number of lipid types and can undergo phase separation with the formation of nanometer-scale liquid-ordered lipid domains, also called rafts. Raft coalescence, i.e., the fusion of lipid domains, is involved in important cell processes, such as signaling and trafficking. In this work, within the framework of the theory of elasticity of lipid membranes, we explore how amphipathic peptides adsorbed on lipid membranes may affect the domain–domain fusion processes. We show that the elastic deformations of lipid membranes drive amphipathic peptides to the boundary of lipid domains, which leads to an increase in the average energy barrier of the domain–domain fusion, even if the surface concentration of amphipathic peptides is low and the domain boundaries are only partially occupied by the peptides. This inhibition of the fusion of lipid domains may lead to negative side effects of using amphipathic peptides as antimicrobial agents. Full article

(This article belongs to the Special Issue Synergy of Proteins, Peptides and Lipid Membranes in Vital Cellular Processes)

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15 pages, 2656 KiB

Open AccessArticle

Electrostatic Potentials Caused by the Release of Protons from Photoactivated Compound Sodium 2-Methoxy-5-nitrophenyl Sulfate at the Surface of Bilayer Lipid Membrane

by Valerij S. Sokolov, Vsevolod Yu. Tashkin, Darya D. Zykova, Yulia V. Kharitonova, Timur R. Galimzyanov and Oleg V. Batishchev

Membranes 2023, 13(8), 722; https://doi.org/10.3390/membranes13080722 - 8 Aug 2023

Viewed by 773

Abstract

Lateral transport and release of protons at the water–membrane interface play crucial roles in cell bioenergetics. Therefore, versatile techniques need to be developed for investigating as well as clarifying the main features of these processes at the molecular level. Here, we experimentally measured the kinetics of binding of protons released from the photoactivated compound sodium 2-methoxy-5-nitrophenyl sulfate (MNPS) at the surface of a bilayer lipid membrane (BLM). We developed a theoretical model of this process describing the damage of MNPS coupled with the release of the protons at the membrane surface, as well as the exchange of MNPS molecules and protons between the membrane and solution. We found that the total change in the boundary potential difference across the membrane, ∆ϕ_b, is the sum of opposing effects of adsorption of MNPS anions and release of protons at the membrane–water interface. Steady-state change in the ∆ϕ_b due to protons decreased with the concentration of the buffer and increased with the pH of the solution. The change in the concentration of protons evaluated from measurements of ∆ϕ_b was close to that in the unstirred water layer near the BLM. This result, as well as rate constants of the proton exchange between the membrane and the bulk solution, indicated that the rate-limiting step of the proton surface to bulk release is the change in the concentration of protons in the unstirred layer. This means that the protons released from MNPS remain in equilibrium between the BLM surface and an adjacent water layer. Full article

(This article belongs to the Special Issue Synergy of Proteins, Peptides and Lipid Membranes in Vital Cellular Processes)

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11 pages, 3897 KiB

Open AccessArticle

Amyloid Precursor Protein Changes Arrangement in a Membrane and Its Structure Depending on the Cholesterol Content

by Vladimir D. Krasnobaev, Yaroslav V. Bershatsky, Olga V. Bocharova, Eduard V. Bocharov and Oleg V. Batishchev

Membranes 2023, 13(8), 706; https://doi.org/10.3390/membranes13080706 - 28 Jul 2023

Cited by 1 | Viewed by 1497

Abstract

One of the hallmarks of Alzheimer’s disease (AD) is the accumulation of amyloid beta (Aβ) peptides in the brain. The processing of amyloid precursor protein (APP) into Aβ is dependent on the location of APP in the membrane, membrane lipid composition and, possibly, presence of lipid rafts. In this study, we used atomic force microscopy (AFM) to investigate the interaction between transmembrane fragment APP_672–726 (corresponding to Aβ_1–55) and its amyloidogenic mutant L723P with membranes combining liquid-ordered and liquid-disordered lipid phases. Our results demonstrated that most of the APP_672–726 is located either in the liquid-disordered phase or at the boundary between ordered and disordered phases, and hardly ever in rafts. We did not notice any major changes in the domain structure induced by APP_672–726. In membranes without cholesterol APP_672–726, and especially its amyloidogenic mutant L723P formed annular structures and clusters rising above the membrane. Presence of cholesterol led to the appearance of concave membrane regions up to 2 nm in depth that were deeper for wild type APP_672–726. Thus, membrane cholesterol regulates changes in membrane structure and permeability induced by APP that might be connected with further formation of membrane pores. Full article

(This article belongs to the Special Issue Synergy of Proteins, Peptides and Lipid Membranes in Vital Cellular Processes)

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Review

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23 pages, 2923 KiB

Open AccessReview

Electric Fields at the Lipid Membrane Interface

by Yury A. Ermakov

Membranes 2023, 13(11), 883; https://doi.org/10.3390/membranes13110883 - 16 Nov 2023

Cited by 1 | Viewed by 1723

Abstract

This review presents a comprehensive analysis of electric field distribution at the water–lipid membrane interface in the context of its relationship to various biochemical problems. The main attention is paid to the methodological aspects of bioelectrochemical techniques and quantitative analysis of electrical phenomena caused by the ionization and hydration of the membrane–water interface associated with the phase state of lipids. One of the objectives is to show the unique possibility of controlling changes in the structure of the lipid bilayer initiated by various membrane-active agents that results in electrostatic phenomena at the surface of lipid models of biomembranes—liposomes, planar lipid bilayer membranes (BLMs) and monolayers. A set of complicated experimental facts revealed in different years is analyzed here in order of increasing complexity: from the adsorption of biologically significant inorganic ions and phase rearrangements in the presence of multivalent cations to the adsorption and incorporation of pharmacologically significant compounds into the lipid bilayer, and formation of the layers of macromolecules of different types. Full article

(This article belongs to the Special Issue Synergy of Proteins, Peptides and Lipid Membranes in Vital Cellular Processes)

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14 pages, 780 KiB

Open AccessReview

Toxic Effects of Penetrating Cations

by Svyatoslav Sokolov, Anna Zyrina, Sergey Akimov, Dmitry Knorre and Fedor Severin

Membranes 2023, 13(10), 841; https://doi.org/10.3390/membranes13100841 - 22 Oct 2023

Cited by 2 | Viewed by 2128

Abstract

As mitochondria are negatively charged organelles, penetrating cations are used as parts of chimeric molecules to deliver specific compounds into mitochondria. In other words, they are used as electrophilic carriers for such chemical moieties as antioxidants, dyes, etc., to transfer them inside mitochondria. However, unmodified penetrating cations affect different aspects of cellular physiology as well. In this review, we have attempted to summarise the data about the side effects of commonly used natural (e.g., berberine) and artificial (e.g., tetraphenylphosphonium, rhodamine, methylene blue) penetrating cations on cellular physiology. For instance, it was shown that such types of molecules can (1) facilitate proton transport across membranes; (2) react with redox groups of the respiratory chain; (3) induce DNA damage; (4) interfere with pleiotropic drug resistance; (5) disturb membrane integrity; and (6) inhibit enzymes. Also, the products of the biodegradation of penetrating cations can be toxic. As penetrating cations accumulate in mitochondria, their toxicity is mostly due to mitochondrial damage. Mitochondria from certain types of cancer cells appear to be especially sensitive to penetrating cations. Here, we discuss the molecular mechanisms of the toxic effects and the anti-cancer activity of penetrating cations. Full article

(This article belongs to the Special Issue Synergy of Proteins, Peptides and Lipid Membranes in Vital Cellular Processes)

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