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State-of-the-Art Antimicrobial Peptides in the Era of Antibiotic Resistance
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State-of-the-Art Antimicrobial Peptides in the Era of Antibiotic Resistance

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: 20 December 2024 | Viewed by 4686

Special Issue Editor

Dr. Surajit Bhattacharjya

E-Mail Website
Guest Editor
School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore
Interests: biomolecular NMR spectroscopy; cell adhesion; antimicrobials
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The surge in antibiotic-resistant bacteria demands the development of new antimicrobials with novel modes of action. Antimicrobial peptides (AMPs) or host defense AMPs have gained high prominence in this regard. AMPs can demonstrate multifunctional activity including the killing of drug-resistant bacterial pathogens, wound healing, antibiotic potentiators (adjuvants), immunomodulation, and endotoxic neutralization. The design, engineering, chemical modifications, and bio-conjugations of AMPs can pave the way for next-generation antimicrobial therapeutics. Template-based design of potent AMPs would require an understating of the mode of action and structural basis of their activity. This Special Issue will focus on atomic-resolution structures and interactions of AMPs with their cognate biological/bacterial targets. Papers presenting the development of novel imaging methods to examine the mode of action and interactions of AMPs are solicited.

Dr. Surajit Bhattacharjya
Guest Editor

Manuscript Submission Information

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Keywords

  • antimicrobial peptides
  • host defense peptides
  • structrues
  • design of antimcrobial peptides
  • membrane interacitons
  • protein complex

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Published Papers (3 papers)

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Research

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21 pages, 2912 KiB  
Article
Role of Peptide Associations in Enhancing the Antimicrobial Activity of Adepantins: Comparative Molecular Dynamics Simulations and Design Assessments
by Matko Maleš, Davor Juretić and Larisa Zoranić
Int. J. Mol. Sci. 2024, 25(22), 12009; https://doi.org/10.3390/ijms252212009 - 8 Nov 2024
Viewed by 606
Abstract
Adepantins are peptides designed to optimize antimicrobial biological activity through the choice of specific amino acid residues, resulting in helical and amphipathic structures. This paper focuses on revealing the atomistic details of the mechanism of action of Adepantins and aligning design concepts with [...] Read more.
Adepantins are peptides designed to optimize antimicrobial biological activity through the choice of specific amino acid residues, resulting in helical and amphipathic structures. This paper focuses on revealing the atomistic details of the mechanism of action of Adepantins and aligning design concepts with peptide behavior through simulation results. Notably, Adepantin-1a exhibits a broad spectrum of activity against both Gram-positive and Gram-negative bacteria, while Adepantin-1 has a narrow spectrum of activity against Gram-negative bacteria. The simulation results showed that one of the main differences is the extent of aggregation. Both peptides exhibit a strong tendency to cluster due to the amphipathicity embedded during design process. However, the more potent Adepantin-1a forms smaller aggregates than Adepantin-1, confirming the idea that the optimal aggregations, not the strongest aggregations, favor activity. Additionally, we show that incorporation of the cell penetration region affects the mechanisms of action of Adepantin-1a and promotes stronger binding to anionic and neutral membranes. Full article
(This article belongs to the Special Issue State-of-the-Art Antimicrobial Peptides in the Era of Antibiotic Resistance)
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17 pages, 3900 KiB  
Article
Outer-Membrane Permeabilization, LPS Transport Inhibition: Activity, Interactions, and Structures of Thanatin Derived Antimicrobial Peptides
by Swaleeha Jaan Abdullah, Bernice Tan Siu Yan, Nithya Palanivelu, Vidhya Bharathi Dhanabal, Juan Pablo Bifani and Surajit Bhattacharjya
Int. J. Mol. Sci. 2024, 25(4), 2122; https://doi.org/10.3390/ijms25042122 - 9 Feb 2024
Cited by 2 | Viewed by 1817
Abstract
Currently, viable antibiotics available to mitigate infections caused by drug-resistant Gram-negative bacteria are highly limited. Thanatin, a 21-residue-long insect-derived antimicrobial peptide (AMP), is a promising lead molecule for the potential development of novel antibiotics. Thanatin is extremely potent, particularly against the Enterobacter group [...] Read more.
Currently, viable antibiotics available to mitigate infections caused by drug-resistant Gram-negative bacteria are highly limited. Thanatin, a 21-residue-long insect-derived antimicrobial peptide (AMP), is a promising lead molecule for the potential development of novel antibiotics. Thanatin is extremely potent, particularly against the Enterobacter group of Gram-negative pathogens, e.g., E. coli and K. pneumoniae. As a mode of action, cationic thanatin efficiently permeabilizes the LPS-outer membrane and binds to the periplasmic protein LptAm to inhibit outer membrane biogenesis. Here, we have utilized N-terminal truncated 16- and 14-residue peptide fragments of thanatin and investigated structure, activity, and selectivity with correlating modes of action. A designed 16-residue peptide containing D-Lys (dk) named VF16 (V1PIIYCNRRT-dk-KCQRF16) demonstrated killing activity in Gram-negative bacteria. The VF16 peptide did not show any detectable toxicity to the HEK 293T cell line and kidney cell line Hep G2. As a mode of action, VF16 interacted with LPS, permeabilizing the outer membrane and binding to LptAm with high affinity. Atomic-resolution structures of VF16 in complex with LPS revealed cationic and aromatic surfaces involved in outer membrane interactions and permeabilization. Further, analyses of an inactive 14-residue native thanatin peptide (IM14: IIYCNRRTGKCQRM) delineated the requirement of the β-sheet structure in activity and target interactions. Taken together, this work would pave the way for the designing of short analogs of thanatin-based antimicrobials. Full article
(This article belongs to the Special Issue State-of-the-Art Antimicrobial Peptides in the Era of Antibiotic Resistance)
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Review

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18 pages, 6220 KiB  
Review
An Overview of Frog Skin-Derived Esc Peptides: Promising Multifunctional Weapons against Pseudomonas aeruginosa-Induced Pulmonary and Ocular Surface Infections
by Maria Luisa Mangoni, Maria Rosa Loffredo, Bruno Casciaro, Loretta Ferrera and Floriana Cappiello
Int. J. Mol. Sci. 2024, 25(8), 4400; https://doi.org/10.3390/ijms25084400 - 16 Apr 2024
Viewed by 1709
Abstract
Antimicrobial resistance is a silent pandemic harming human health, and Pseudomonas aeruginosa is the most common bacterium responsible for chronic pulmonary and eye infections. Antimicrobial peptides (AMPs) represent promising alternatives to conventional antibiotics. In this review, the in vitro/in vivo activities of the [...] Read more.
Antimicrobial resistance is a silent pandemic harming human health, and Pseudomonas aeruginosa is the most common bacterium responsible for chronic pulmonary and eye infections. Antimicrobial peptides (AMPs) represent promising alternatives to conventional antibiotics. In this review, the in vitro/in vivo activities of the frog skin-derived AMP Esc(1-21) are shown. Esc(1-21) rapidly kills both the planktonic and sessile forms of P. aeruginosa and stimulates migration of epithelial cells, likely favoring repair of damaged tissue. However, to undertake preclinical studies, some drawbacks of AMPs (cytotoxicity, poor biostability, and limited delivery to the target site) must be overcome. For this purpose, the stereochemistry of two amino acids of Esc(1-21) was changed to obtain the diastereomer Esc(1-21)-1c, which is more stable, less cytotoxic, and more efficient in treating P. aeruginosa-induced lung and cornea infections in mouse models. Incorporation of these peptides (Esc peptides) into nanoparticles or immobilization to a medical device (contact lens) was revealed to be an effective strategy to ameliorate and/or to prolong the peptides’ antimicrobial efficacy. Overall, these data make Esc peptides encouraging candidates for novel multifunctional drugs to treat lung pathology especially in patients with cystic fibrosis and eye dysfunctions, characterized by both tissue injury and bacterial infection. Full article
(This article belongs to the Special Issue State-of-the-Art Antimicrobial Peptides in the Era of Antibiotic Resistance)
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