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Proteins and Peptides Self-Assemblies: Synthesis, Structural Elucidation and Functional Properties

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (31 August 2023) | Viewed by 3596

Special Issue Editor


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Guest Editor
Dipartimento di Scienza e Alta Tecnologia, Università degli Studi dell’Insubria, Via Valleggio 11, 22100 Como, Italy
Interests: bio-active peptides; self-assembly peptides; peptide-based conjugates for drug delivery; peptidomimetics; targeting protein–protein interactions; organometallic chemistry in nitrogen-containing heterocycles

Special Issue Information

Dear Colleagues,

The self-assembly of biomolecules is a naturally occurring process in living cells that provides complex superstructures which have a multitude of essential biological functions. At the same time; protein or peptide aggregation and complexation in structures such as fibrils or amyloid oligomers is often related to the development of several diseases for which efficient treatments are still needed. In recent decades; the elucidation of the structural bases that generate these highly ordered; three-dimensional supramolecular assemblies; strongly dependent on specific peptide sequences; was achieved using novel therapeutic agents targeting protein–protein interactions as well as novel peptide-based biomaterials. In this context; the study of self-assembling peptides that aggregate in controllable nanosystems such as fibers; micelles; and gels has recently emerged as an exciting direction of research to fabricate biocompatible systems for drug delivery and tissue engineering. As a consequence; the investigation of protein/peptide self-assembly represents an important field of research; the outcomes of which can offer new opportunities in the fields of drug discovery and biomaterials development.

The purpose of this Special Issue is to collect an interdisciplinary overview of recent progress in the synthesis; structure and functional elucidation of protein and peptide self-assembly in supramolecular functional systems. We invite you to submit contributions in the form of reviews or original research articles that provide new insights into this intriguing research area.

Dr. Silvia Gazzola
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. Molecules is an international peer-reviewed open access semimonthly 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

  • self-assembling peptides
  • supramolecular peptide nanostructures
  • structure elucidation
  • protein self-assembly and aggregation
  • computational approaches in the design of self-assembling peptides
  • peptide-based functional materials
  • targeting protein–protein assemblies and aggregates
  • biomolecular vehicles for drug delivery
  • nanofibers
  • nanotubes and gels

Published Papers (2 papers)

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Research

20 pages, 7905 KiB  
Article
A Novel Antimicrobial Peptide, Dermaseptin-SS1, with Anti-Proliferative Activity, Isolated from the Skin Secretion of Phyllomedusa tarsius
by Xiaonan Ma, Yuping Chen, Anmei Shu, Yangyang Jiang, Xiaoling Chen, Chengbang Ma, Mei Zhou, Tao Wang, Tianbao Chen, Chris Shaw and Lei Wang
Molecules 2023, 28(18), 6558; https://doi.org/10.3390/molecules28186558 - 11 Sep 2023
Viewed by 1798
Abstract
The emergence of multidrug-resistant bacteria has severely increased the burden on the global health system, and such pathogenic infections are considered a great threat to human well-being. Antimicrobial peptides, due to their potent antimicrobial activity and low possibility of inducing resistance, are increasingly [...] Read more.
The emergence of multidrug-resistant bacteria has severely increased the burden on the global health system, and such pathogenic infections are considered a great threat to human well-being. Antimicrobial peptides, due to their potent antimicrobial activity and low possibility of inducing resistance, are increasingly attracting great interest. Herein, a novel dermaseptin peptide, named Dermaseptin-SS1 (SS1), was identified from a skin-secretion-derived cDNA library of the South/Central American tarsier leaf frog, Phyllomedusa tarsius, using a ‘shotgun’ cloning strategy. The chemically synthesized peptide SS1 was found to be broadly effective against Gram-negative bacteria with low haemolytic activity in vitro. A designed synthetic analogue of SS1, named peptide 14V5K, showed lower salt sensitivity and more rapid bacteria killing compared to SS1. Both peptides employed a membrane-targeting mechanism to kill Escherichia coli. The antiproliferative activity of SS1 and its analogues against lung cancer cell lines was found to be significant. Full article
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15 pages, 3930 KiB  
Article
Nanoparticles Carrying Conserved Regions of Influenza A Hemagglutinin, Nucleoprotein, and M2 Protein Elicit a Strong Humoral and T Cell Immune Response and Protect Animals from Infection
by Anna A. Zykova, Elena A. Blokhina, Liudmila A. Stepanova, Marina A. Shuklina, Olga O. Ozhereleva, Liudmila M. Tsybalova, Victor V. Kuprianov and Nikolai V. Ravin
Molecules 2023, 28(18), 6441; https://doi.org/10.3390/molecules28186441 - 5 Sep 2023
Cited by 1 | Viewed by 1330
Abstract
Current influenza vaccines are mainly strain-specific and have limited efficacy in preventing new influenza A strains. Efficient control of infection can potentially be achieved through the development of broad-spectrum vaccines based on conserved antigens. A combination of several such antigens, including the conserved [...] Read more.
Current influenza vaccines are mainly strain-specific and have limited efficacy in preventing new influenza A strains. Efficient control of infection can potentially be achieved through the development of broad-spectrum vaccines based on conserved antigens. A combination of several such antigens, including the conserved region of the second subunit of the hemagglutinin (HA2), the extracellular domain of the M2 protein (M2e), and epitopes of nucleoprotein (NP), which together can elicit an antibody- and cell-mediated immune response, would be preferred for vaccine development. In this study, we obtained recombinant virus-like particles formed by an artificial self-assembling peptide (SAP) carrying two epitopes from NP, tandem copies of M2e and HA2 peptides, along with a T helper Pan DR-binding epitope (PADRE). Fusion proteins expressed in Escherichia coli self-assembled in vitro into spherical particles with a size of 15–35 nm. Immunization of mice with these particles induced strong humoral immune response against M2e and the entire virus, and lead to the formation of cytokine-secreting antigen-specific CD4+ and CD8+ effector memory T cells. Immunization provided high protection of mice against the lethal challenge with the influenza A virus. Our results show that SAP-based nanoparticles carrying conserved peptides from M2, HA, and NP proteins of the influenza A virus, as well as T helper epitope PADRE, can be used for the development of universal flu vaccines. Full article
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