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Arginine Homopeptide of 11 Residues as a Model of Cell-Penetrating Peptides in the Interaction with Bacterial Membranes

Aróstica, Mónica ; Rojas, Roberto ; Aguilar, Luis Felipe ; Carvajal-Rondanelli, Patricio ; Albericio, Fernando ; Guzmán, Fanny ; Cárdenas, Constanza

Membranes (Basel), 2022-11, Vol.12 (12), p.1180 [Revista revisada por pares]

Switzerland: MDPI AG

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Arginine Homopeptide of 11 Residues as a Model of Cell-Penetrating Peptides in the Interaction with Bacterial Membranes
Autor: Aróstica, Mónica ; Rojas, Roberto ; Aguilar, Luis Felipe ; Carvajal-Rondanelli, Patricio ; Albericio, Fernando ; Guzmán, Fanny ; Cárdenas, Constanza
Materias: Amino acids ; Analysis ; Antibacterial activity ; antibacterial assays ; Antibacterial materials ; Antibiotics ; Antimicrobial activity ; Antimicrobial agents ; Arginine ; arginine homopeptide ; Bacteria ; circular dichroism ; Drug resistance in microorganisms ; E coli ; Escherichia coli ; Gram-positive bacteria ; Interaction models ; Lipids ; Membrane vesicles ; Membranes ; model membrane interactions ; Nitrogen ; Peptides ; Polyproline ; Protein structure ; Residues ; Secondary structure ; secondary structure PPII ; Staphylococcus aureus
Es parte de: Membranes (Basel), 2022-11, Vol.12 (12), p.1180
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descripción: Cell-penetrating peptides rich in arginine are good candidates to be considered as antibacterial compounds, since peptides have a lower chance of generating resistance than commonly used antibiotics. Model homopeptides are a useful tool in the study of activity and its correlation with a secondary structure, constituting an initial step in the construction of functional heteropeptides. In this report, the 11-residue arginine homopeptide (R11) was used to determine its antimicrobial activity against and and the effect on the secondary structure, caused by the substitution of the arginine residue by the amino acids Ala, Pro, Leu and Trp, using the scanning technique. As a result, most of the substitutions improved the antibacterial activity, and nine peptides were significantly more active than R11 against the two tested bacteria. The cell-penetrating characteristic of the peptides was verified by SYTOX green assay, with no disruption to the bacterial membranes. Regarding the secondary structure in four different media-PBS, TFE, membrane extracts and DMPG vesicles-the polyproline II structure, the one of the parent R11, was not altered by unique substitutions, although the secondary structure of the peptides was best defined in membrane extract. This work aimed to shed light on the behavior of the interaction model of penetrating peptides and bacterial membranes to enhance the development of functional heteropeptides.
Editor: Switzerland: MDPI AG
Idioma: Inglés

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Arginine Homopeptide of 11 Residues as a Model of Cell-Penetrating Peptides in the Interaction with Bacterial Membranes

Aróstica, Mónica ; Rojas, Roberto ; Aguilar, Luis Felipe ; Carvajal-Rondanelli, Patricio ; Albericio, Fernando ; Guzmán, Fanny ; Cárdenas, Constanza

Switzerland: MDPI AG

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