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Antibiotics
Special Issues
Design, Synthesis, and Application of Antimicrobial Peptides
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Design, Synthesis, and Application of Antimicrobial Peptides

A special issue of Antibiotics (ISSN 2079-6382). This special issue belongs to the section "Antimicrobial Peptides".

Deadline for manuscript submissions: closed (15 September 2023) | Viewed by 4436

Special Issue Editor

Dr. Natalia Molchanova

E-Mail Website
Guest Editor
The Molecular Foundry, Lawrence Berkely National Laboratory, Berkeley, CA 94720, USA
Interests: peptides; peptide mimics; antimicrobials; organic synthesis; multi-drug resistance

Special Issue Information

Dear Colleagues,

The search for efficient antimicrobial therapies to treat infections caused by resistant bacteria is in higher demand than ever before. The prolonged use of existing antibiotics has contributed to the development and spread of drug-resistant microorganisms that add a significant and increasing burden to healthcare and society. Antimicrobial peptides (AMPs) found in the innate immune system of different organisms present a promising class of bioactive compounds that offers a potential solution to the antibiotic resistance problem due to their mode of action on microbial membranes. Bacterial failure to develop resistance against most antimicrobial peptides has made them an efficient tool which can impact the new era of antimicrobials. However, natural AMPs that are present in living organisms are not stable and can display elevated toxicity and hemolytic profiles. Therefore, it is necessary to implement rational design strategies to synthetic AMPs to overcome these disadvantages and further modify the chemical and physical properties of existing peptides. Hence, this Special Issue seeks manuscript submissions that further our understanding of the correlation between the design of peptides and their therapeutic profiles.

Dr. Natalia Molchanova
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. Antibiotics 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 2900 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

  • antimicrobial peptides
  • antimicrobial resistance
  • peptide interaction with bacteria
  • peptide diversity
  • synthetic peptides

Published Papers (2 papers)

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Research

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21 pages, 3286 KiB  
Article
A Novel Strategy for the Design of Aurein 1.2 Analogs with Enhanced Bioactivities by Conjunction of Cell-Penetrating Regions
by Fengting Liao, Yuping Chen, Anmei Shu, Xiaoling Chen, Tao Wang, Yangyang Jiang, Chengbang Ma, Mei Zhou, Tianbao Chen, Chris Shaw and Lei Wang
Antibiotics 2023, 12(2), 412; https://doi.org/10.3390/antibiotics12020412 - 19 Feb 2023
Cited by 1 | Viewed by 1779
Abstract
The rational design modification of membrane-active peptide structures by introducing additional membrane-penetrating regions has become a good strategy for the improvement of action and potency. Aurein 1.2 (GLFDIIKKIAESF-NH2) is a multifunctional antimicrobial peptide isolated from the green and golden bell frog, [...] Read more.
The rational design modification of membrane-active peptide structures by introducing additional membrane-penetrating regions has become a good strategy for the improvement of action and potency. Aurein 1.2 (GLFDIIKKIAESF-NH2) is a multifunctional antimicrobial peptide isolated from the green and golden bell frog, Litoria aurea, and the southern bell frog Litoria raniformis skin secretions. Its bio-functionality has been widely investigated. However, its lack of a potent action failed to provide aurein 1.2 with a competitive edge for further development as a therapeutic agent for clinical use. Herein, aurein 1.2 was chosen as a template for rational modification to achieve a more potent bio-functionality. KLA-2 (GLFDIIKKLAKLAESF-NH2), which a double KLA region inserted into the sequence, presented a 2–16-fold enhancement of antimicrobial activity, a 2–8-fold greater anti-biofilm activity (including biofilm prevention and eradication), and a 7-fold more potent anti-proliferation activity and hence was regarded as the most broad-spectrum active peptide. Additionally, with respect to antimicrobial activity, the IIKK-modified analog, IK-3 (GLFDIIKKIIKKIIKKI-NH2), also demonstrated a potent enhancement of activity against various pathogens, exhibiting a 2–8-fold enhanced activity compared to the parent peptide. Moreover, the selectivities of KLA-1 and KLA-2 were enhanced significantly. In conclusion, peptide modification, through the introduction of additional membrane penetrating regions, can increase both the potency and activity spectra of natural template peptides, making them suitable candidates for new drug development. Full article
(This article belongs to the Special Issue Design, Synthesis, and Application of Antimicrobial Peptides)
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12 pages, 1420 KiB  
Perspective
Engineering Approaches for the Development of Antimicrobial Peptide-Based Antibiotics
by Su-Jin Kang, So Hee Nam and Bong-Jin Lee
Antibiotics 2022, 11(10), 1338; https://doi.org/10.3390/antibiotics11101338 - 30 Sep 2022
Cited by 15 | Viewed by 2202
Abstract
Antimicrobial peptides (AMPs) have received increasing attention as potential alternatives for future antibiotics because of the rise of multidrug-resistant (MDR) bacteria. AMPs are small cationic peptides with broad-spectrum antibiotic activities and different action mechanisms to those of traditional antibiotics. Despite the desirable advantages [...] Read more.
Antimicrobial peptides (AMPs) have received increasing attention as potential alternatives for future antibiotics because of the rise of multidrug-resistant (MDR) bacteria. AMPs are small cationic peptides with broad-spectrum antibiotic activities and different action mechanisms to those of traditional antibiotics. Despite the desirable advantages of developing peptide-based antimicrobial agents, the clinical applications of AMPs are still limited because of their enzymatic degradation, toxicity, and selectivity. In this review, structural modifications, such as amino acid substitution, stapling, cyclization of peptides, and hybrid AMPs with conventional antibiotics or other peptides, will be presented. Additionally, nanodelivery systems using metals or lipids to deliver AMPs will be discussed based on the structural properties and action mechanisms of AMPs. Full article
(This article belongs to the Special Issue Design, Synthesis, and Application of Antimicrobial Peptides)
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