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Membranes
Special Issues
Protein–Lipid Interactions: Recent Studies, Perspectives, and Challenges
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Protein–Lipid Interactions: Recent Studies, Perspectives, and Challenges

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

Deadline for manuscript submissions: closed (30 January 2024) | Viewed by 4234

Special Issue Editors

Dr. Daria N. Melnikova

E-Mail Website
Guest Editor
Shemyakin Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia
Interests: plant innate immunity; plant lipid binding proteins; recombinant expression of proteins; plant allergens; membrane permeability; drug delivery systems
Dr. Oleg V. Batishchev

E-Mail Website
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
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We are pleased to invite you to this Special Issue on “Protein–Lipid Interactions: Recent Studies, Perspectives, and Challenges”. Biological membranes are complex heterogeneous systems composed of lipids, proteins, and carbohydrates. Membranes facilitate essential biological functions that are driven by protein–lipid interactions, in a highly dynamic manner. Nevertheless, many questions related to the chemistry and physics of lipids and proteins are still not understood today. The lack of proper understanding of molecular mechanisms important for the functioning of the biological membranes also hinders practical applications in the industries.

This Special Issue aims to analyze and cover a broad spectrum of protein–lipid interactions and present new information in this area of research. Data on the organizational principles of cell membranes, the structure and function of membrane and lipid binding proteins, the mechanistic details of these interactions, and the study of protein–lipid interplay in vital biological functions may be presented.

For this Special Issue of Membranes, authors are invited to present their recent results, and both original papers and reviews are welcome.

We look forward to receiving your contributions.

Dr. Daria N. Melnikova
Dr. Oleg V. Batishchev
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 and protein–ligand interactions
  • membrane proteins
  • lipid binding proteins
  • membrane protein structure–function relationship
  • membrane permeability
  • membrane transport mechanism
  • dynamic molecular processes
  • structure modeling

Published Papers (3 papers)

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Research

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14 pages, 1172 KiB  
Article
Phospholipid Membrane Interactions of Model Ac-WL-X-LL-OH Peptides Investigated by Solid-State Nuclear Magnetic Resonance
by Nicolai Etwin Alsaker, Øyvind Halskau, Bengt Erik Haug, Nathalie Reuter and Willy Nerdal
Membranes 2024, 14(5), 105; https://doi.org/10.3390/membranes14050105 - 1 May 2024
Viewed by 682
Abstract
The role of aromatic amino acids in peripheral protein membrane binding has been reported to involve cation–π interactions with choline lipids. In this study, we have investigated the interactions of the model pentapeptide Ac-WL-X-LL-OH (where X = L, Y, F, or W) with [...] Read more.
The role of aromatic amino acids in peripheral protein membrane binding has been reported to involve cation–π interactions with choline lipids. In this study, we have investigated the interactions of the model pentapeptide Ac-WL-X-LL-OH (where X = L, Y, F, or W) with the phospholipid membrane using solid-state NMR. The effect of guest residue X on the peptide-lipid interactome was complementary to the seminal report on the interfacial hydrophobicity scale by Wimley and White. We found that the phospholipids retained a lamellar phase in the presence of each of the peptides with an aromatic X residue, whereas the Leu peptide perturbed the bilayer to an extent where an additional isotropic phase was observed. The solid-state NMR 13C and 31P data provide additional information on the influence of these short peptides on the membrane that has not been previously reported. The magnitude of membrane perturbation was in the order of guest residue X = L > Y~F > W, which is consistent with the relative amino acid interfacial affinity reported by Wimley and White. Further work is, however, required to uncover the behavior of the peptide and localization in the membrane domain due to ambiguity of the 13C NMR data. We have launched efforts in this regard for the objective of better understanding the role of aromatic amino acids in peripheral membrane protein binding. Full article
(This article belongs to the Special Issue Protein–Lipid Interactions: Recent Studies, Perspectives, and Challenges)
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Review

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12 pages, 1756 KiB  
Review
Alternative Targets for sPLA2 Activity: Role of Membrane-Enzyme Interactions
by Anna S. Alekseeva and Ivan A. Boldyrev
Membranes 2023, 13(7), 618; https://doi.org/10.3390/membranes13070618 - 23 Jun 2023
Viewed by 1187
Abstract
The secreted phospholipases A2 (sPLA2s) play important roles both physiologically and pathologically, with their expression increasing significantly in diseases such as sepsis, inflammation, different cancers, glaucoma, obesity, Alzheimer’s disease and even COVID-19. The fact has led to a large-scale search for inhibitors of [...] Read more.
The secreted phospholipases A2 (sPLA2s) play important roles both physiologically and pathologically, with their expression increasing significantly in diseases such as sepsis, inflammation, different cancers, glaucoma, obesity, Alzheimer’s disease and even COVID-19. The fact has led to a large-scale search for inhibitors of these enzymes. In total, several dozen promising molecules have been proposed, but not a single one has successfully passed clinical trials. The failures in clinical studies motivated in-depth fundamental studies of PLA2s. Here we review alternative ways to control sPLA2 activity, outside its catalytic site. The concept can be realized by preventing sPLA2 from attaching to the membrane surface; by binding to an external protein which blocks sPLA2 hydrolytic activity; by preventing sPLA2 from orienting properly on the membrane surface; and by preventing substrate binding to the enzyme, keeping the catalytic site unaltered. Evidence in the literature is summarized in the review with the aim to serve as a starting point for new types of sPLA2 inhibitors. Full article
(This article belongs to the Special Issue Protein–Lipid Interactions: Recent Studies, Perspectives, and Challenges)
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17 pages, 760 KiB  
Review
Features and Possible Applications of Plant Lipid-Binding and Transfer Proteins
by Daria N. Melnikova, Ekaterina I. Finkina, Ivan V. Bogdanov, Andrey A. Tagaev and Tatiana V. Ovchinnikova
Membranes 2023, 13(1), 2; https://doi.org/10.3390/membranes13010002 - 20 Dec 2022
Cited by 5 | Viewed by 1542
Abstract
In plants, lipid trafficking within and inside the cell is carried out by lipid-binding and transfer proteins. Ligands for these proteins are building and signaling lipid molecules, secondary metabolites with different biological activities due to which they perform diverse functions in plants. Many [...] Read more.
In plants, lipid trafficking within and inside the cell is carried out by lipid-binding and transfer proteins. Ligands for these proteins are building and signaling lipid molecules, secondary metabolites with different biological activities due to which they perform diverse functions in plants. Many different classes of such lipid-binding and transfer proteins have been found, but the most common and represented in plants are lipid transfer proteins (LTPs), pathogenesis-related class 10 (PR-10) proteins, acyl-CoA-binding proteins (ACBPs), and puroindolines (PINs). A low degree of amino acid sequence homology but similar spatial structures containing an internal hydrophobic cavity are common features of these classes of proteins. In this review, we summarize the latest known data on the features of these protein classes with particular focus on their ability to bind and transfer lipid ligands. We analyzed the structural features of these proteins, the diversity of their possible ligands, the key amino acids participating in ligand binding, the currently known mechanisms of ligand binding and transferring, as well as prospects for possible application. Full article
(This article belongs to the Special Issue Protein–Lipid Interactions: Recent Studies, Perspectives, and Challenges)
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