Antimicrobial Agents and Nanomaterials—2nd Edition

Abstract submission deadline

31 October 2026

Manuscript submission deadline

31 December 2026

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Topic Information

Dear Colleagues,

Antimicrobial resistance (AMR) has come to represent a major problem that has been demonstrated across healthcare settings worldwide. AMR is caused by multidrug-resistant (MDR) microorganisms, or “superbugs”, which can evade many of the antibiotics used in clinical practice. Today, MDR microorganisms constitute a great clinical and economic burden. In fact, the current methods of clinical treatment have started to rely on more aggressive antibiotic therapy, leading to a decrease in the life quality of the infected patients and an increase in the associated therapeutic costs. Due to the failure of conventional antibiotics, we are now entering a new era of clinical treatment based on compounds. This is reflected, for example, in the development of antibacterial nanomaterials or nanoantibiotics. This Topic aims to identify the novel strategies that may be used to overcome AMR, with a particular focus on the development of medical nanomaterials. Topics of interest include, but are not limited to, the following:

• Antimicrobial polymers;
• Antimicrobial peptides and peptidomimetics;
• Synergic effects of antimicrobial agents;
• Antimicrobial coatings;
• Inhibitors of virulence factors;
• Drug nanodelivery systems.

We welcome the contributions of authors working in this critical field of research.

Prof. Dr. Vasco D. B. Bonifácio
Dr. Sandra Pinto
Topic Editors

Keywords

Participating Journals

Journal Name	Impact Factor	CiteScore	Launched Year	First Decision (median)	APC
Biomolecules biomolecules	4.8	9.2	2011	19.4 Days	CHF 2700	Submit
International Journal of Molecular Sciences ijms	4.9	9.0	2000	20.5 Days	CHF 2900	Submit
Micro micro	1.9	3.2	2021	28.1 Days	CHF 1200	Submit
Molecules molecules	4.6	8.6	1996	16.1 Days	CHF 2700	Submit
Antibiotics antibiotics	4.6	8.7	2012	15 Days	CHF 2900	Submit
Nanomaterials nanomaterials	4.3	9.2	2010	15.4 Days	CHF 2400	Submit
Microorganisms microorganisms	4.2	7.7	2013	15.2 Days	CHF 2700	Submit
Journal of Functional Biomaterials jfb	5.2	6.8	2010	15.9 Days	CHF 2700	Submit

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Open AccessArticle

Structural and Functional Effects of the Interaction Between an Antimicrobial Peptide and Its Analogs with Model Bacterial and Erythrocyte Membranes

by Michele Lika Furuya, Gustavo Penteado Carretero, Marcelo Porto Bemquerer, Sumika Kiyota, Magali Aparecida Rodrigues, Tarcillo José de Nardi Gaziri, Norma Lucia Buritica Zuluaga, Danilo Kiyoshi Matsubara, Marcio Nardelli Wandermuren, Karin do Amaral Riske, Hernan Chaimovich, Shirley Schreier and Iolanda Midea Cuccovia

Biomolecules 2025, 15(8), 1143; https://doi.org/10.3390/biom15081143 - 7 Aug 2025

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Abstract

Antimicrobial peptides (AMPs) are a primary defense against pathogens. Here, we examined the interaction of two BP100 analogs, R²R⁵-BP100 (where Arg substitutes Lys 2 and 5) and R²R⁵-BP100-A-NH-C₁₆ (where an Ala and a C [...] Read more.

Antimicrobial peptides (AMPs) are a primary defense against pathogens. Here, we examined the interaction of two BP100 analogs, R²R⁵-BP100 (where Arg substitutes Lys 2 and 5) and R²R⁵-BP100-A-NH-C₁₆ (where an Ala and a C₁₆ hydrocarbon chain are added to the R²R⁵-BP100 C-terminus), with membrane models. Large unilamellar vesicles (LUVs) and giant unilamellar vesicles (GUVs) were prepared with the major lipids in Gram-positive (GP) and Gram-negative (GN) bacteria, as well as red blood cells (RBCs). Fluorescence data, dynamic light scattering (DLS), and zeta potential measurements revealed that upon achieving electroneutrality through peptide binding, vesicle aggregation occurred. Circular dichroism (CD) spectra corroborated these observations, and upon vesicle binding, the peptides acquired α-helical conformation. The peptide concentration, producing a 50% release of carboxyfluorescein (C₅₀) from LUVs, was similar for GP-LUVs. With GN and RBC-LUVs, C₅₀ decreased in the following order: BP100 > R²R⁵-BP100 > R²R⁵BP100-A-NH-C₁₆. Optical microscopy of GP-, GN-, and RBC-GUVs revealed the rupture or bursting of the two former membranes, consistent with a carpet mechanism of action. Using GUVs, we confirmed RBC aggregation by BP100 and R²R⁵-BP100. We determined the minimal inhibitory concentrations (MICs) of peptides for a GN bacterium (Escherichia coli (E. coli)) and two GP bacteria (two strains of Staphylococcus aureus (S. aureus) and one strain of Bacillus subtilis (B. subtilis)). The MICs for S. aureus were strain-dependent. These results demonstrate that Lys/Arg replacement can improve the parent peptide’s antimicrobial activity while increasing hydrophobicity renders the peptide less effective and more hemolytic. Full article

(This article belongs to the Topic Antimicrobial Agents and Nanomaterials—2nd Edition)

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