Previous Article in Journal
Internalizing and Externalizing Traits During Adolescence: Using Epigenetics and Perinatal Risks to Differentiate Clusters of Symptoms
 
 
Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
Journals
Biomolecules
Volume 15
Issue 8
10.3390/biom15081143
biomolecules-logo
Submit to this Journal Review for this Journal Propose a Special Issue
► Article Menu

Article Menu

share Share announcement Help format_quote Cite
first_page
settings
Order Article Reprints
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
This is an early access version, the complete PDF, HTML, and XML versions will be available soon.
Article

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

by
Michele Lika Furuya
1,
Gustavo Penteado Carretero
1,2,
Marcelo Porto Bemquerer
3,
Sumika Kiyota
4,
Magali Aparecida Rodrigues
1,
Tarcillo José de Nardi Gaziri
1,
Norma Lucia Buritica Zuluaga
1,
Danilo Kiyoshi Matsubara
1,
Marcio Nardelli Wandermuren
5,
Karin do Amaral Riske
6,
Hernan Chaimovich
1,
Shirley Schreier
1,* and
Iolanda Midea Cuccovia
1,*
1
Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo 05508-220, Brazil
2
Department of Science and Environment, Roskilde University, 4000 Roskilde, Denmark
3
Embrapa Gado de Leite, Juiz de Fora, Minas Gerais 36038-330, Brazil
4
Laboratório de Bioquímica de Proteínas e Peptídeos, Instituto Biológico, São Paulo 04014-002, Brazil
5
Instituto de Química, Universidade de São Paulo, São Paulo 05508-220, Brazil
6
6 Departamento de Biofísica, Universidade Federal de São Paulo, São Paulo 04026-002, Brazil
*
Authors to whom correspondence should be addressed.
Biomolecules 2025, 15(8), 1143; https://doi.org/10.3390/biom15081143 (registering DOI)
Submission received: 19 June 2025 / Revised: 25 July 2025 / Accepted: 4 August 2025 / Published: 7 August 2025
(This article belongs to the Topic Antimicrobial Agents and Nanomaterials—2nd Edition)
Review Reports Versions Notes

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 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.
Keywords: antimicrobial peptides; model bacterial membranes; model red cell membranes; large unilamellar vesicles; giant unilamellar vesicles antimicrobial peptides; model bacterial membranes; model red cell membranes; large unilamellar vesicles; giant unilamellar vesicles

Share and Cite

MDPI and ACS Style

Furuya, M.L.; Carretero, G.P.; Bemquerer, M.P.; Kiyota, S.; Rodrigues, M.A.; Gaziri, T.J.d.N.; Zuluaga, N.L.B.; Matsubara, D.K.; Wandermuren, M.N.; Riske, K.d.A.; et al. Structural and Functional Effects of the Interaction Between an Antimicrobial Peptide and Its Analogs with Model Bacterial and Erythrocyte Membranes. Biomolecules 2025, 15, 1143. https://doi.org/10.3390/biom15081143

AMA Style

Furuya ML, Carretero GP, Bemquerer MP, Kiyota S, Rodrigues MA, Gaziri TJdN, Zuluaga NLB, Matsubara DK, Wandermuren MN, Riske KdA, et al. Structural and Functional Effects of the Interaction Between an Antimicrobial Peptide and Its Analogs with Model Bacterial and Erythrocyte Membranes. Biomolecules. 2025; 15(8):1143. https://doi.org/10.3390/biom15081143

Chicago/Turabian Style

Furuya, Michele Lika, 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, and et al. 2025. "Structural and Functional Effects of the Interaction Between an Antimicrobial Peptide and Its Analogs with Model Bacterial and Erythrocyte Membranes" Biomolecules 15, no. 8: 1143. https://doi.org/10.3390/biom15081143

APA Style

Furuya, M. L., Carretero, G. P., Bemquerer, M. P., Kiyota, S., Rodrigues, M. A., Gaziri, T. J. d. N., Zuluaga, N. L. B., Matsubara, D. K., Wandermuren, M. N., Riske, K. d. A., Chaimovich, H., Schreier, S., & Cuccovia, I. M. (2025). Structural and Functional Effects of the Interaction Between an Antimicrobial Peptide and Its Analogs with Model Bacterial and Erythrocyte Membranes. Biomolecules, 15(8), 1143. https://doi.org/10.3390/biom15081143

Note that from the first issue of 2016, this journal uses article numbers instead of page numbers. See further details here.

Article Metrics

Back to TopTop