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Digital, Currently, the detection of pathogens such as Escherichia coli through instrumental alternatives with fast response and excellent sensitivity and selectivity are being studied. Biosensors are systems consisting of nanomaterials and biomolecules that exhibit remarkable properties such as simplicity, portable, affordable, user‑friendly, and deliverable to end‑users. For this, in this work we report for the first time, to our knowledge, the bioinformatic design of a new peptide based on TIR protein, a receptor of Intimin membrane protein which is characteristic of E. coli. This peptide (named PEPTIR‑1.0) was used as recognition element in a biosensor based on AuNPs‑modified screen‑printed electrodes for the detection of E. coli. The morphological and electrochemical characteristics of the biosensor obtained were studied. Results show that the biosensor can detect the bacteria with limits of detection and quantification of 2 and 6 CFU/mL, respectively. Moreover, the selectivity of the system is statistically significant towards the detection of the pathogen in the presence of other microorganisms such as P. aeruginosa and S. aureus. This makes this new PEPTIR‑1.0 based biosensor can be used in the rapid, sensitive, and selective detection of E. coli in aqueous matrices., Ciencias Exactas y Naturales

Digital, Antimicrobial peptides arise as a very promising alternative for the treatment of infections generated by pathogenic microorganisms. The Ib-M2 antimicrobial peptide turns out to be a very promising candidate for these types of applications. However, it is required to evaluate immobilization systems that give peptides greater stability and activity in order to be used in biological systems. Given the above, this paper reports the preparation of superparamagnetic iron oxide nanoparticles (SPIONs) coated with chitosan in order to immobilize the Ib-M2 antimicrobial peptide. Structural properties of SPIONs were studied by DLS, SEM, XRD, FT-IR, XPS and the magnetic properties were evaluated by vibrating-sample magnetometer technique. The antimicrobial activity of the Ib-M2/SPIONs@Chi bioconjugate obtained was evaluated against Escherichia coli O157:H7 by determining the minimum inhibitory concentration (MIC). Results show that the SPIONs obtained have particle size between 10 and 15 nm with a magnetite-type structure which was confirmed by FT-IR and XPS. Characterization of magnetic properties evidences a superparamagnetic behavior of nanoparticles obtained. MIC results showed that Ib-M2/SPIONs@Chi bioconjugate exhibit a comparable or higher activity against E. coli in comparison with the free Ib-M2 peptide. These results show that the bioconjugate obtained can be considered for use in biomedical applications., Ciencias básicas biomédicas, epidemiología, salud pública enfermedades infecciosas, enfermedades no transmisibles epidemiología, salud y desarrollo, discapacidad, Ciencias Básicas y Aplicadas para la Sostenibilidad

1 p., El desarrollo de nuevos péptidos antimicrobianos se ha convertido en una alternativa atractiva a los antibióticos convencionales debido a las crecientes tasas de resistencia a los fármacos microbianos. Ib-M corresponde a una familia de péptidos sintéticos catiónicos, de 20 aminoácidos de longitud, que han mostrado efecto inhibidor frente a la cepa no patógena Escherichia coli K-12. Este trabajo evaluó el potencial antimicrobiano de los péptidos Ib-M contra el E patógeno . coli O157: H7 utilizando una cepa de referencia y un aislado clínico. Los péptidos Ib-M mostraron actividad antibacteriana contra ambas cepas de E . coliO157: H7; la concentración mínima inhibitoria de los péptidos Ib-M osciló entre 1,6 y 12,5 µM y la concentración bactericida mínima osciló entre 3,7 y 22,9 µM, siendo Ib-M1 e Ib-M2 los péptidos que presentaron mayor efecto inhibidor. El ensayo de cinética de eliminación del tiempo mostró una reducción de la población bacteriana en más del 95% después de 4 horas de exposición a 1xMIC de Ib-M1. Se observó una baja citotoxicidad en células VERO con una concentración citotóxica del 50% en el rango de 197,5 a más de 400 μM. Todos los péptidos mostraron una estructura aleatoria en ambientes hidrófilos, excepto Ib-M1, y todos ellos pasaron a una estructura α-helicoidal cuando se incrementó la hidrofobicidad del medio. En conclusión, estos hallazgos apoyan el efecto antimicrobiano in vitro de los péptidos Ib-M contra las bacterias patógenas.E . coli O157: H7 y resultan ser moléculas prometedoras para el desarrollo de nuevas alternativas terapéuticas., The development of new antimicrobial peptides has become an attractive alternative to conventional antibiotics due to the increasing rates of microbial drug resistance. Ib-M corresponds to a family of cationic synthetic peptides, 20 amino acids in length, that have shown inhibitory effect against the non-pathogenic strain Escherichia coli K-12. This work evaluated the antimicrobial potential of Ib-M peptides against the pathogenic E. coli O157: H7 using a reference strain and a clinical isolate. The Ib-M peptides showed antibacterial activity against both strains of E. coli O157: H7; the minimum inhibitory concentration of Ib-M peptides ranged from 1.6 to 12.5 μM and the minimum bactericidal concentration ranged from 3.7 to 22.9 μM, being Ib-M1 and Ib-M2 the peptides that presented the highest inhibitory effect. Time-kill kinetics assay showed a reduction of the bacterial population by more than 95% after 4 hours of exposure to 1xMIC of Ib-M1. Low cytotoxicity was observed in VERO cells with 50% cytotoxic concentration in the range from 197.5 to more than 400 μM. All peptides showed a random structure in hydrophilic environments, except Ib-M1, and all of them transitioned to an α-helical structure when the hydrophobicity of the medium was increased. In conclusion, these findings support the in vitro antimicrobial effect of Ib-M peptides against the pathogenic bacteria E. coli O157: H7 and prove to be promising molecules for the development of new therapeutic alternatives., Ej. 1

The Ib-M6 peptide has antibacterial activity against non-pathogenic Escherichia coli K-12 strain. The first part of this study determines the antibacterial activity of Ib-M6 against fourteen pathogenic strains of E. coli O157:H7. Susceptibility assay showed that Ib-M6 had values of Minimum Inhibitory Concentration (MIC) lower than streptomycin, used as a reference antibiotic. Moreover, to predict the possible interaction between Ib-M6 and outer membrane components of E. coli, we used molecular docking simulations where FhuA protein and its complex with Lipopolysaccharide (LPS&ndash, FhuA) were used as targets of the peptide. FhuA/Ib-M6 complexes had energy values between &minus, 39.5 and &minus, 40.5 Rosetta Energy Units (REU) and only one hydrogen bond. In contrast, complexes between LPS&ndash, FhuA and Ib-M6 displayed energy values between &minus, 25.6 and &minus, 40.6 REU, and the presence of five possible hydrogen bonds. Hence, the antimicrobial activity of Ib-M6 peptide shown in the experimental assays could be caused by its interaction with the outer membrane of E. coli.

Digital, The encapsulation of Ib-M6 antibacterial peptide in pellets of polyvinyl alcohol (PVA) and polyvinyl alcoholalginate (PVA-Alg) matrices was carried out in order to explore its controlled release and activity against Escherichia coli K-12. The pellets were obtained by combined ice segregation induced self-assembly (ISISA) and freezing-thawing methods and their microstructure was studied by scanning electron microscopy. Bromothymol blue was used as a model compound to study the transport mechanisms and release from pellets. The results show that there is a significant effect of the total concentration of PVA precursor solutions, the mass ratio of PVA of different molecular weights and the addition of alginate on the microstructure and transport properties of pellets. The antibacterial activity of Ib-M6 against Escherichia coli K-12 was not affected by the encapsulation in PVA pellets. However, the release of Ib-M6 from PVA-Alg pellets was not possible, probably due to the electrostatic interaction of positively charged Ib-M6 and negatively alginate structure. Nonetheless, the controlled release of Ib-M6 from polymeric matrices can be fitting by modifying parameters such as the concentration and type of polymer precursors., 1 ed., Ciencias Basicas y Aplicadas para la Sostenibilidad

Polyvinyl alcohol (PVA) porous carriers were prepared by means of ice templating of aqueous solutions containing of 90 kD and/or 16 kD PVA. The carriers were loaded with traces of a colored probe (methyl orange) to screen their release properties, once immersed in water. The carriers prepared from solutions containing 90 kD and 16 kD PVA resulted in intimate polymer mixtures, exhibiting physical properties that stand in between those of the bare 90 kD or 16 kD PVA end members. The freezing protocols employed were adapted to prepare carriers textured in the form of either monolithic scaffolds (directional constant freezing rate) or millimetric pellets (flash-freeze). Monolithic carriers remain stable in aqueous solution, and the probe release is governed by a swelling-diffusion mechanism. The kinetics of probe release can be tuned from minutes to hours by either increasing the total PVA content or the 90 kD-to-16 kD PVA ratio in the parent solution. In contrast, pellets (millimetric carriers) immersed in water release the probe on the scale of minutes, irrespective of the PVA content or composition. However, the PVA content and the 90 kD-to-16 kD PVA ratio dramatically affect the stability of the carriers. Depending on the formulation, these small carriers can develop swelling, erosion, or eventually massive dissolution. Fil: Sonego, Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina Fil: Flórez Castillo, Johanna M.. Universidad Industrial Santander; Colombia Fil: Jobbagy, Matias. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina

A family of Ib-AMP4 peptide analogues was obtained by solid phase synthesis, modifying the net charge and hydrophobicity of C-terminal domain by replacing certain amino acidic residues by arginine and tryptophan. Additionally, disulfide bonds were eliminated by replacing the cysteine residues by methionine, which resulted in a decrease in the number of synthesis byproducts, and consequently diminished the subsequent purification steps. The obtained peptides were purified by RP-HPLC and their molecular mass was determined by MALDI-TOF mass spectrometry. The peptide analogues (IC50 between 1 and 50 μM) presented a higher antibacterial activity against Escherichia coli K-12 than the native peptide (IC50 > 100 μM). The hemolytic activity of the peptide with the highest antibacterial efficacy presented no degradation of erythrocytes for a concentration of 1 μM that corresponds to its IC50 value. The results show that the synthesized peptides are good candidates for the treatment of diseases caused by E. coli. Fil: Flórez Castillo, J. M.. Universidad Industrial Santander; Colombia Fil: Perullini, Ana Mercedes. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina Fil: Jobbagy, Matias. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina Fil: Cano Calle, Herminsul de Jesús. Universidad Industrial Santander; Colombia