Use este identificador para citar ou linkar para este item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1178765
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dc.contributor.authorFURUYA, M. L.
dc.contributor.authorCARRETERO, G. P.
dc.contributor.authorBEMQUERER, M. P.
dc.contributor.authorKIYOTA, S.
dc.contributor.authorRODRIGUES, M. A.
dc.contributor.authorGAZIRI, T. J. de N.
dc.contributor.authorZULUAGA, N. L. B.
dc.contributor.authorMATSUBARA, D. K.
dc.contributor.authorWANDERMUREN, M. N.
dc.contributor.authorRISKE, K. A.
dc.contributor.authorCHAIMOVICH, H.
dc.contributor.authorSCHREIER, S.
dc.contributor.authorCUCCOVIA, I. M.
dc.date.accessioned2025-09-15T03:51:52Z-
dc.date.available2025-09-15T03:51:52Z-
dc.date.created2025-09-14
dc.date.issued2025
dc.identifier.citationBiomolecules, v. 15, 1143, 2025.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1178765-
dc.descriptionAntimicrobial peptides (AMPs) are a primary defense against pathogens. Here, we examined the interaction of two BP100 analogs, R2R 5 -BP100 (where Arg substitutes Lys 2 and 5) and R2R 5 -BP100-A-NH-C16 (where an Ala and a C16 hydrocarbon chain are added to the R 2R 5 -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 > R2R 5 -BP100 > R2R 5BP100-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 R2R 5 -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.
dc.language.isoeng
dc.rightsopenAccess
dc.subjectVesícula unilamelar
dc.subjectHemácia
dc.titleStructural and functional effects of the interaction between an antimicrobial peptide and its analogs with model bacterial and erythrocyte membranes.
dc.typeArtigo de periódico
dc.subject.thesagroPeptídeo
dc.subject.thesagroBactéria
dc.subject.thesagroMembrana
dc.subject.nalthesaurusAntimicrobial peptides
riaa.ainfo.id1178765
riaa.ainfo.lastupdate2025-09-14
dc.identifier.doihttps://doi.org/10.3390/biom15081143
dc.contributor.institutionMICHELE LIKA FURUYA, UNIVERSIDADE DE SÃO PAULO; GUSTAVO PENTEADO CARRETERO, UNIVERSIDADE DE SÃO PAULO; MARCELO PORTO BEMQUERER, CNPGL; SUMIKA KIYOTA, INSTITUTO BIOLÓGICO; MAGALI APARECIDA RODRIGUES, UNIVERSIDADE DE SÃO PAULO; TARCILLO JOSÉ DE NARDI GAZIRI, UNIVERSIDADE DE SÃO PAULO; NORMA LUCIA BURITICA ZULUAGA, UNIVERSIDADE DE SÃO PAULO; DANILO KIYOSHI MATSUBARA, UNIVERSIDADE DE SÃO PAULO; MARCIO NARDELLI WANDERMUREN, UNIVERSIDADE DE SÃO PAULO; KARIN A. RISKE, UNIVERSIDADE FEDERAL DE SÃO PAULO; HERNAN CHAIMOVICH, UNIVERSIDADE DE SÃO PAULO; SHIRLEY SCHREIER, UNIVERSIDADE DE SÃO PAULO; IOLANDA MIDEA CUCCOVIA, UNIVERSIDADE DE SÃO PAULO.
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