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Membranes
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Membrane Interaction between Lipids, Proteins and Peptides
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Membrane Interaction between Lipids, Proteins and Peptides

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 September 2023) | Viewed by 8946

Special Issue Editor

Dr. John Tien Jui Cheng

E-Mail Website
Guest Editor
1. Center for Microbial Diseases and Immunity Research, Department of Microbiology and Immunology, University of British Columbia, 232-2259 Lower Mall, Vancouver, BC V6T 1Z4, Canada
2. Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC V6T 1Z1, Canada
3. Department of Biochemistry and Molecular Biology, Life Sciences Centre, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC V6T 1Z3, Canada
Interests: physical biochemistry; protein biochemistry; peptide chemistry; lipid biochemistry; membrane biochemistry; membrane biophysics; antimicrobial peptide; peptide–membrane interaction; structural biology; drug discovery; clinical translation

Special Issue Information

Dear Colleagues,

We are pleased to invite you to submit a paper to our Special Issue titled “Membrane Interaction between Lipids, Proteins and Peptides”.

Lipid membranes play critical roles in cell survival. As dull as it may seem, we cannot deny the essential existence of the lipid membranes that enclose all cellular components, regardless of whether they are important or unimportant. These membranes represent the first line of defense against foreign invaders (toxins, pathogens, etc.), much like how the base, walls, and roof of a house shelter residents. Over the years, many researchers have invested a vast amount of effort into understanding various cellular components and machineries (e.g., nuclear/genetic materials, proteins (complexes), and small (bio)molecule functional entities). By doing so, we seem to show a higher level of appreciation for the kitchen or living room than for the walls of the house, indirectly marginalizing the comfort and security provided by the walls, base, and roof.

Interestingly, most researchers seem to recognize proteins (receptors) as the determining factor(s) of any bimolecular interaction between molecules (including organics, inorganics, peptides, and proteins) and lipid membranes, and lipid membranes act as facilitators to capitalize on these interactions. Very few have appreciated lipid membranes as independent contributors or maybe even as drivers in these interactions.

Based on these observations, I would like to propose a Special Issue that emphasizes peptide–membrane interactions and or/ protein (receptor)–membrane interactions from a lipid membrane-oriented perspective (i.e., focusing on how lipid membranes actively participate and effects these interactions, or, an even more daring concept—if lipid membranes actually direct these biomolecule–lipid membrane interaction events in some way). The reason why I propose this topic is that most researchers focus on biomolecules and treat lipid membranes as a subsidiary, but I believe that lipid membranes can actually play major directing and/or deciding role(s) in these interactions, and I would like to challenge researchers to re-evaluate our views on these biological events.

This Special Issue will serve as a perfect foundation to collect and document non-traditional developments, unconventional innovations, and non-classical concepts on peptide– and/or protein–membrane interactions. We invite authors to submit their latest findings to challenge our traditional views; both original papers and reviews are welcome. Research areas may include (but are not limited to) the following: lipid–lipid, peptide–membrane, and protein–membrane interactions; solid-state methods to study/characterize these interactions; classical and/or novel physical biochemistry approaches to identify novel interactions; advances in biophysical approaches to identify important biomembrane contributions in these interactions and related biological events; novel views on known biological events thar arise from these interactions using different approaches; and the discovery of new biological events resulting from these interactions. 

I look forward to receiving your contributions.

Dr. John Tien Jui Cheng
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

  • lipid membranes
  • lipid membrane biochemistry
  • membrane biophysics
  • peptide–membrane interactions
  • protein (receptor)–membrane interactions
  • unconventional concepts

Published Papers (6 papers)

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Research

13 pages, 5277 KiB  
Article
Effect of CM15 on Supported Lipid Bilayer Probed by Atomic Force Microscopy
by Olivia D. Walsh, Leona Choi and Krishna P. Sigdel
Membranes 2023, 13(11), 864; https://doi.org/10.3390/membranes13110864 - 28 Oct 2023
Viewed by 1458
Abstract
Antimicrobial peptides are key components of the immune system. These peptides affect the membrane in various ways; some form nano-sized pores, while others only produce minor defects. Since these peptides are increasingly important in developing antimicrobial drugs, understanding the mechanism of their interactions [...] Read more.
Antimicrobial peptides are key components of the immune system. These peptides affect the membrane in various ways; some form nano-sized pores, while others only produce minor defects. Since these peptides are increasingly important in developing antimicrobial drugs, understanding the mechanism of their interactions with lipid bilayers is critical. Here, using atomic force microscopy (AFM), we investigated the effect of a synthetic hybrid peptide, CM15, on the membrane surface comprising E. coli polar lipid extract. Direct imaging of supported lipid bilayers exposed to various concentrations of the peptide revealed significant membrane remodeling. We found that CM15 interacts with supported lipid bilayers and forms membrane-spanning defects very quickly. It is found that CM15 is capable of remodeling both leaflets of the bilayer. For lower CM15 concentrations, punctate void-like defects were observed, some of which re-sealed themselves as a function of time. However, for CM15 concentrations higher than 5 µM, the defects on the bilayers became so widespread that they disrupted the membrane integrity completely. This work enhances the understanding of CM15 interactions with the bacterial lipid bilayer. Full article
(This article belongs to the Special Issue Membrane Interaction between Lipids, Proteins and Peptides)
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11 pages, 4665 KiB  
Article
Insights into Early Steps of Decanoic Acid Self-Assemblies under Prebiotic Temperatures Using Molecular Dynamics Simulations
by Romina V. Sepulveda, Christopher Sbarbaro, Ma Cecilia Opazo, Yorley Duarte, Fernando González-Nilo and Daniel Aguayo
Membranes 2023, 13(5), 469; https://doi.org/10.3390/membranes13050469 - 28 Apr 2023
Viewed by 1244
Abstract
The origin of life possibly required processes in confined systems that facilitated simple chemical reactions and other more complex reactions impossible to achieve under the condition of infinite dilution. In this context, the self-assembly of micelles or vesicles derived from prebiotic amphiphilic molecules [...] Read more.
The origin of life possibly required processes in confined systems that facilitated simple chemical reactions and other more complex reactions impossible to achieve under the condition of infinite dilution. In this context, the self-assembly of micelles or vesicles derived from prebiotic amphiphilic molecules is a cornerstone in the chemical evolution pathway. A prime example of these building blocks is decanoic acid, a short-chain fatty acid capable of self-assembling under ambient conditions. This study explored a simplified system made of decanoic acids under temperatures ranging from 0 °C to 110 °C to replicate prebiotic conditions. The study revealed the first point of aggregation of decanoic acid into vesicles and examined the insertion of a prebiotic-like peptide in a primitive bilayer. The information gathered from this research provides critical insights into molecule interactions with primitive membranes, allowing us to understand the first nanometric compartments needed to trigger further reactions that were essential for the origin of life. Full article
(This article belongs to the Special Issue Membrane Interaction between Lipids, Proteins and Peptides)
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13 pages, 4460 KiB  
Article
The Role of C2 Domains in Two Different Phosphatases: PTEN and SHIP2
by Laura H. John, Fiona B. Naughton, Mark S. P. Sansom and Andreas Haahr Larsen
Membranes 2023, 13(4), 408; https://doi.org/10.3390/membranes13040408 - 04 Apr 2023
Cited by 2 | Viewed by 1380
Abstract
Phosphatase and tensin homologue (PTEN) and SH2-containing inositol 5′-phosphatase 2 (SHIP2) are structurally and functionally similar. They both consist of a phosphatase (Ptase) domain and an adjacent C2 domain, and both proteins dephosphorylate phosphoinositol-tri(3,4,5)phosphate, PI(3,4,5)P3; PTEN at the 3-phophate and SHIP2 [...] Read more.
Phosphatase and tensin homologue (PTEN) and SH2-containing inositol 5′-phosphatase 2 (SHIP2) are structurally and functionally similar. They both consist of a phosphatase (Ptase) domain and an adjacent C2 domain, and both proteins dephosphorylate phosphoinositol-tri(3,4,5)phosphate, PI(3,4,5)P3; PTEN at the 3-phophate and SHIP2 at the 5-phosphate. Therefore, they play pivotal roles in the PI3K/Akt pathway. Here, we investigate the role of the C2 domain in membrane interactions of PTEN and SHIP2, using molecular dynamics simulations and free energy calculations. It is generally accepted that for PTEN, the C2 domain interacts strongly with anionic lipids and therefore significantly contributes to membrane recruitment. In contrast, for the C2 domain in SHIP2, we previously found much weaker binding affinity for anionic membranes. Our simulations confirm the membrane anchor role of the C2 domain in PTEN, as well as its necessity for the Ptase domain in gaining its productive membrane-binding conformation. In contrast, we identified that the C2 domain in SHIP2 undertakes neither of these roles, which are generally proposed for C2 domains. Our data support a model in which the main role of the C2 domain in SHIP2 is to introduce allosteric interdomain changes that enhance catalytic activity of the Ptase domain. Full article
(This article belongs to the Special Issue Membrane Interaction between Lipids, Proteins and Peptides)
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12 pages, 2087 KiB  
Article
A Simple, Semi-Quantitative Acyl Biotin Exchange-Based Method to Detect Protein S-Palmitoylation Levels
by Valentina Buffa, Giorgia Adamo, Sabrina Picciotto, Antonella Bongiovanni and Daniele P. Romancino
Membranes 2023, 13(3), 361; https://doi.org/10.3390/membranes13030361 - 21 Mar 2023
Cited by 1 | Viewed by 1959
Abstract
Protein S-palmitoylation is a reversible post-translational lipidation in which palmitic acid (16:0) is added to protein cysteine residue by a covalent thioester bond. This modification plays an active role in membrane targeting of soluble proteins, protein–protein interaction, protein trafficking, and subcellular localization. Moreover, [...] Read more.
Protein S-palmitoylation is a reversible post-translational lipidation in which palmitic acid (16:0) is added to protein cysteine residue by a covalent thioester bond. This modification plays an active role in membrane targeting of soluble proteins, protein–protein interaction, protein trafficking, and subcellular localization. Moreover, palmitoylation is related to different diseases, such as neurodegenerative pathologies, cancer, and developmental defects. The aim of this research is to provide a straightforward and sensitive procedure to detect protein palmitoylation based on Acyl Biotin Exchange (ABE) chemistry. Our protocol setup consists of co-immunoprecipitation of native proteins (i.e., CD63), followed by the direct detection of palmitoylation on proteins immobilized on polyvinylidene difluoride (PVDF) membranes. With respect to the conventional ABE-based protocol, we optimized and validated a rapid semi-quantitative assay that is shown to be significantly more sensitive and highly reproducible. Full article
(This article belongs to the Special Issue Membrane Interaction between Lipids, Proteins and Peptides)
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13 pages, 4946 KiB  
Article
Effects of a Pseudomonas Strain on the Lipid Transfer Proteins, Appoplast Barriers and Activity of Aquaporins Associated with Hydraulic Conductance of Pea Plants
by Elena Martynenko, Tatiana Arkhipova, Guzel Akhiyarova, Guzel Sharipova, Ilshat Galin, Oksana Seldimirova, Ruslan Ivanov, Tatiana Nuzhnaya, Ekaterina Finkina, Tatiana Ovchinnikova and Guzel Kudoyarova
Membranes 2023, 13(2), 208; https://doi.org/10.3390/membranes13020208 - 08 Feb 2023
Cited by 4 | Viewed by 1118
Abstract
Lipid transfer proteins (LTPs) are known to be involved in suberin deposition in the Casparian bands of pea roots, thereby reinforcing apoplast barriers. Moreover, the Pseudomonas mandelii IB-Ki14 strain accelerated formation of the Casparian bands in wheat plants, although involvement of LTPs in [...] Read more.
Lipid transfer proteins (LTPs) are known to be involved in suberin deposition in the Casparian bands of pea roots, thereby reinforcing apoplast barriers. Moreover, the Pseudomonas mandelii IB-Ki14 strain accelerated formation of the Casparian bands in wheat plants, although involvement of LTPs in the process was not studied. Here, we investigated the effects of P. mandelii IB-Ki14 on LTPs, formation of the Casparian bands, hydraulic conductance and activity of aquaporins (AQPs) in pea plants. RT PCR showed a 1.6-1.9-fold up-regulation of the PsLTP-coding genes and an increase in the abundance of LTP proteins in the phloem of pea roots induced by the treatment with P. mandelii IB-Ki14. The treatment was accompanied with increased deposition of suberin in the Casparian bands. Hydraulic conductance did not decrease in association with the bacterial treatment despite strengthening of the apoplast barriers. At the same time, the Fenton reagent, serving as an AQPs inhibitor, decreased hydraulic conductance to a greater extent in treated plants relative to the control group, indicating an increase in the AQP activity by the bacteria. We hypothesize that P. mandelii IB-Ki14 stimulates deposition of suberin, in the biosynthesis of which LTPs are involved, and increases aquaporin activity, which in turn prevents a decrease in hydraulic conductance due to formation of the apoplast barriers in pea roots. Full article
(This article belongs to the Special Issue Membrane Interaction between Lipids, Proteins and Peptides)
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8 pages, 1146 KiB  
Article
Interaction Energy between Two Separated Charged Spheres Surrounded Inside and Outside by Electrolyte
by István P. Sugár
Membranes 2022, 12(10), 947; https://doi.org/10.3390/membranes12100947 - 28 Sep 2022
Viewed by 1131
Abstract
By using the recently generalized version of Newton’s shell theorem, analytical equations are derived to calculate the electric interaction energy between two separated, charged spheres surrounded outside and inside by electrolyte. This electric interaction energy is calculated as a function of the electrolyte’s [...] Read more.
By using the recently generalized version of Newton’s shell theorem, analytical equations are derived to calculate the electric interaction energy between two separated, charged spheres surrounded outside and inside by electrolyte. This electric interaction energy is calculated as a function of the electrolyte’s ion concentration, temperature, distance between the spheres and size of the spheres. At the same distance between the spheres, the absolute value of the interaction energy decreases with increasing electrolyte ion concentration and increases with increasing temperature. At zero electrolyte ion concentration, the derived analytical equation transforms into the Coulomb Equation Finally, the analytical equation is generalized to calculate the electric interaction energy of N separated, charged spheres surrounded by electrolyte. Full article
(This article belongs to the Special Issue Membrane Interaction between Lipids, Proteins and Peptides)
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