Membrane-Interacting Diagnostic/Therapeutic Peptides in Infectious Diseases and Oncology

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 (20 May 2023) | Viewed by 2297

Special Issue Editors


E-Mail Website
Guest Editor
Innovative Immunological Models Unit, Istituto Nazionale Tumori IRCCS Fondazione Pascale, 80131 Naples, Italy
Interests: bioactive peptides; peptide drug development; peptide drug conjugate; anticancer peptides; peptides in diagnosis and therapy
Special Issues, Collections and Topics in MDPI journals

E-Mail Website
Guest Editor
Molecular Biology and Viral Oncology Unit, Istituto Nazionale Tumori IRCCS Fondazione Pascale, 80131 Naples, Italy
Interests: oncology; molecular biology; virology; biochemistry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In the era of drug resistance (against bacteria and chemotherapeutics), membrane-active peptides play an important role in the design and development of new drugs.

Currently, chemotherapy is the prevailing therapeutic strategy for the systemic treatment of infections and cancer. Unfortunately, the inappropriate use of antibiotics is reducing their effectiveness by selecting highly resistant pathogens on the one hand, and on the other antiblastic chemotherapy is non-selective and causes many side effects on normal cells, particularly bone-marrow and high replicating tissues (including gastrointestinal tract and reproductive organs). Furthermore, anti-bacterial and antiblastic chemotherapeutic molecules induce and activate the expression of multi-drug resistance (MDR) reducing the activity of chemotherapeutic groups of drugs. The most relevant goal of the scientific community is to develop drugs that can specifically target or infected or neoplastic cells, with limited cytotoxicity on normal cells, as well as pathogens. Peptides can bind with high affinity membrane receptors activating molecular pathways or can be internalised by endocytic processes targeting cells expressing specific protein on their surface. Further changes of the leader sequence allow the entrance of peptides through the plasma membrane and their compartmentalization into the nuclear and/or the mitochondrial membrane inducing cancer cells apoptosis or cell cycle modulation, as well as cytotoxic T lymphocytes (CTLs) recognition. Such peptides can be also used for drug delivery. The main advantages of peptide-based drugs are the ease of development, low costs, the possibility of increasing the chemical-physical and enzymatic stability, mainly related to the conformation and the amino acid composition, respectively.

To broaden the number of peptide applications of the current special issue, several topics will be considered including antimicrobial peptides, cell penetrating peptides, anticancer peptides, glycopeptides, membrane-acting peptides, interfering peptides, peptides mimotopes of oncoprotein, peptide-driven cellular immunity. Authors are invited to submit their latest results. Both original papers and reviews are welcome.

Dr. Anna Lucia Tornesello
Dr. Franco M. Buonaguro
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

  • anticancer peptides
  • bioactive peptides
  • cell penetrating peptides
  • antimicrobial peptides
  • cells membrane
  • membrane models
  • membrane translocating peptides
  • membrane-active proteins
  • radiolabeled peptides
  • nanocarriers
  • theranostics
  • peptide-dependent cellular immunity

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:

Research

19 pages, 3425 KiB  
Article
Antimicrobial Peptide Mastoparan-AF Kills Multi-Antibiotic Resistant Escherichia coli O157:H7 via Multiple Membrane Disruption Patterns and Likely by Adopting 3–11 Amphipathic Helices to Favor Membrane Interaction
by Chun-Hsien Lin, Ching-Lin Shyu, Zong-Yen Wu, Chao-Min Wang, Shiow-Her Chiou, Jiann-Yeu Chen, Shu-Ying Tseng, Ting-Er Lin, Yi-Po Yuan, Shu-Peng Ho, Kwong-Chung Tung, Frank Chiahung Mao, Han-Jung Lee and Wu-Chun Tu
Membranes 2023, 13(2), 251; https://doi.org/10.3390/membranes13020251 - 20 Feb 2023
Cited by 4 | Viewed by 1402
Abstract
We investigated the antimicrobial activity and membrane disruption modes of the antimicrobial peptide mastoparan-AF against hemolytic Escherichia coli O157:H7. Based on the physicochemical properties, mastoparan-AF may potentially adopt a 3–11 amphipathic helix-type structure, with five to seven nonpolar or hydrophobic amino acid residues [...] Read more.
We investigated the antimicrobial activity and membrane disruption modes of the antimicrobial peptide mastoparan-AF against hemolytic Escherichia coli O157:H7. Based on the physicochemical properties, mastoparan-AF may potentially adopt a 3–11 amphipathic helix-type structure, with five to seven nonpolar or hydrophobic amino acid residues forming the hydrophobic face. E. coli O157:H7 and two diarrheagenic E. coli veterinary clinical isolates, which are highly resistant to multiple antibiotics, are sensitive to mastoparan-AF, with minimum inhibitory and bactericidal concentrations (MIC and MBC) ranging from 16 to 32 μg mL−1 for E. coli O157:H7 and four to eight μg mL−1 for the latter two isolates. Mastoparan-AF treatment, which correlates proportionally with membrane permeabilization of the bacteria, may lead to abnormal dents, large perforations or full opening at apical ends (hollow tubes), vesicle budding, and membrane corrugation and invagination forming irregular pits or pores on E. coli O157:H7 surface. In addition, mRNAs of prepromastoparan-AF and prepromastoparan-B share a 5′-poly(A) leader sequence at the 5′-UTR known for the advantage in cap-independent translation. This is the first report about the 3–11 amphipathic helix structure of mastoparans to facilitate membrane interaction. Mastoparan-AF could potentially be employed to combat multiple antibiotic-resistant hemolytic E. coli O157:H7 and other pathogenic E. coli. Full article
Show Figures

Figure 1

Back to TopTop