Autores
J. Hernandez-Montelongo(a)(b)(c), Y.R. Corrales Ureña(d), D. Machado(e), M. Lancelloti(e), M.P. Pinheiro(f), K. Rischka(f), P.N. Lisboa-Filho(g), M.A. Cotta(a).
(a) Departamento de Física Aplicada, Instituto de Física Gleb Wataghin, Universidade Estadual de Campinas, 13083-859 Campinas, Brazil.
(b) Departamento de Ciencias Matemáticas y Físicas, Facultad de Ingeniería, Universidad Católica de Temuco, 4813302 Temuco, Chile.
(c) Núcleo de Investigación en Bioprodructos y Materiales Avanzados (BioMa), Facultad de Ingeniería, Universidad Católica de Temuco, 4781312 Temuco, Chile.
(d) Laboratorio Nacional de Nanotecnología, Centro Nacional de Alta Tecnología, 1174-1200 San José, Costa Rica.
(e) Faculdade de Ciências Farmacêuticas, Universidade Estadual de Campinas, 13083-871 Campinas, Brazil.
(f) Fraunhofer Institute for Manufacturing Technology and Advanced Materials, 28359 Bremen, Germany.
(g) Departamento de Física, Faculdade de Ciências, Universidade Estadual Paulista, 17033-360 Bauru, Brazil.
COLLOIDS AND SURFACES B: BIOINTERFACES.
Volumen: 164 Páginas: 370-378.
DOI: https://doi.org/10.1016/j.colsurfb.2018.02.002
Fecha de Publicación: 05 de Febrero de 2018
Abstract
Staphylococcus epidermidis is a gram-positive bacterium, and one of the most prevalent causes of nosocomial infections due to its strong ability to form biofilms on catheters and surgical implants. Here we explore the antimicrobial properties of Tet-124 peptides, which are part of the innate defense against different multicellular organisms in nature. Two different Tet-124 peptides were immobilized on a polyethylenimine (PEI) film to determine their impact on the antimicrobial properties: KLWWMIRRW (Tet-124), which contains only natural amino acids, and KLWWMIRRWG-(F-Br)-G (F-Br = 4-Bromophenylalanine), a modified Tet-124 sequence with the addition of an unnatural amino acid. The immobilization was obtained as a result of the electrostatic interaction between PEI amino groups and the C-terminal carboxylic groups of tryptophan and glycine amino acids of Tet-124 and Tet-124-Br peptides, respectively. The process was monitored and studied by water contact angle, Atomic Force Microscopy (AFM), X-ray Photoelectron Spectroscopy (XPS) and Quartz Crystal Microbalance with Dissipation (QCM-D) measurements. The antibacterial effect of our samples against S. epidermis was evaluated by the spread plate counting method, and cytotoxicity was tested using fibroblast cultures. Our results indicate the feasibility to immobilize electrostatically both Tet-124 peptides for biomedical applications.