Structure-Function Relationships and Biological Processes of Membrane Proteins

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

Deadline for manuscript submissions: 31 May 2024 | Viewed by 3506

Special Issue Editor


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Guest Editor
Department of Science of Agriculture, Food, Natural Resources and Engineering, University of Foggia, 71122 Foggia, Italy
Interests: model membranes; membrane biophysics; lipid–protein interaction; ion-channel-forming peptides and their biophysical characterization; natural bioactive compounds

Special Issue Information

Dear Colleagues,

Research on membrane proteins has always been a topic of great interest among researchers. In recent years, there has been an increased focus on this field of study thanks to modern investigation techniques. The biological processes involving membrane proteins are manifold—transport, signal transduction, cell recognition, intra- and extracellular adhesion, enzymatic activity—and consist of many biochemical reactions or other events that are essential for the life of an organism and for its ability to interact with the external environment. Both membrane proteins and those that interact with the lipid bilayer show a close relationship between the structure, function, and biological processes related to them. The amino acid sequence determines the protein folding, and the three-dimensional structure, in turn, determines the specific biological activity, which contributes to the correct realization of biological processes. Misfolded membrane proteins can cause instability and lead to various diseases.
The Special Issue, entitled "Structure–Function Relationships and Biological Processes of Membrane Proteins", aims to present the recent progress in the structure–function study of membrane proteins concerning the biological processes in which they are involved. Topics include, but are not limited to, new results in channel proteins, transporters, receptors, adhesion proteins, and membrane enzymes, obtained with different investigation techniques on both in vitro and in vivo systems.

Authors are invited to submit their latest findings; both original papers and reviews are welcome.

We are looking forward to receiving your contributions.

Dr. Daniela Meleleo
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

  • structure and organization of membrane proteins
  • structure-function relationship
  • interaction of membrane proteins with bilayer lipids
  • molecular mechanisms
  • modeling and simulation
  • biophysics

Published Papers (2 papers)

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Research

18 pages, 2604 KiB  
Article
The Effect of Calcium Ions on hIAPP Channel Activity: Possible Implications in T2DM
by Daniela Meleleo, Giuseppe Cibelli, Anna Valenzano, Maria Mastrodonato and Rosanna Mallamaci
Membranes 2023, 13(11), 878; https://doi.org/10.3390/membranes13110878 - 09 Nov 2023
Cited by 1 | Viewed by 1525
Abstract
The calcium ion (Ca2+) has been linked to type 2 diabetes mellitus (T2DM), although the role of Ca2+ in this disorder is the subject of intense investigation. Serum Ca2+ dyshomeostasis is associated with the development of insulin resistance, reduced [...] Read more.
The calcium ion (Ca2+) has been linked to type 2 diabetes mellitus (T2DM), although the role of Ca2+ in this disorder is the subject of intense investigation. Serum Ca2+ dyshomeostasis is associated with the development of insulin resistance, reduced insulin sensitivity, and impaired glucose tolerance. However, the molecular mechanisms involving Ca2+ ions in pancreatic β-cell loss and subsequently in T2DM remain poorly understood. Implicated in the decline in β-cell functions are aggregates of human islet amyloid polypeptide (hIAPP), a small peptide secreted by β-cells that shows a strong tendency to self-aggregate into β-sheet-rich aggregates that evolve toward the formation of amyloid deposits and mature fibrils. The soluble oligomers of hIAPP can permeabilize the cell membrane by interacting with bilayer lipids. Our study aimed to evaluate the effect of Ca2+ on the ability of the peptide to incorporate and form ion channels in zwitterionic planar lipid membranes (PLMs) composed of palmitoyl-oleoyl-phosphatidylcholine (POPC) and on the aggregation process of hIAPP molecules in solution. Our results may help to clarify the link between Ca2+ ions, hIAPP peptide, and consequently the pathophysiology of T2DM. Full article
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26 pages, 18195 KiB  
Article
Influence of Intramineral Proteins on the Growth of Carbonate Crystals Using as a Scaffold Membranes of Ratite Birds and Crocodiles Eggshells
by Nerith R. Elejalde-Cadena, Denisse Hernández, Francesco Capitelli, Selene R. Islas, Maria J. Rosales-Hoz, Michele Zema, Serena C. Tarantino, Dritan Siliqi and Abel Moreno
Membranes 2023, 13(11), 869; https://doi.org/10.3390/membranes13110869 - 01 Nov 2023
Viewed by 1655
Abstract
The lack of information on structural basis where proteins are involved, as well as the biomineralization processes of different systems such as bones, diatom frustules, and eggshells, have intrigued scientists from different fields for decades. This scientific curiosity has led to the use [...] Read more.
The lack of information on structural basis where proteins are involved, as well as the biomineralization processes of different systems such as bones, diatom frustules, and eggshells, have intrigued scientists from different fields for decades. This scientific curiosity has led to the use of methodologies that help understand the mechanism involved in the formation of these complex structures. Therefore, this work focuses on the use of eggshell membranes from different species of ratites (emu and ostrich) and reptiles (two species of crocodiles) as a model to differentiate biocalcification and biosilicification by introducing calcium phosphate or silica inside the membrane fiber mantles. We performed this to obtain information about the process of eggshell formation as well as the changes that occur in the membrane during crystal formation. In order to identify and understand the early processes leading to the formation of the microstructures present in the eggshell, we decided to carry out the synthesis of silica-carbonate of calcium, barium, and strontium called biomorph in the presence of intramineral proteins. This was carried out to evaluate the influence of these proteins on the formation of specific structures. We found that the proteins on untreated membranes, present a structural growth similar to those observed in the inner part of the eggshell, while in treated membranes, the structures formed present a high similarity with those observed in the outer and intermediate part of the eggshell. Finally, a topographic and molecular analysis of the biomorphs and membranes was performed by scanning electron microscopy (SEM), Raman and Fourier-transform Infrared (FTIR) spectroscopies. Full article
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