EVALUACIÓN DEL DIRECCIONAMIENTO ELECTROQUÍMICO DE PROTEÍNAS SOBRE RECUBRIMIENTOS DE ÁCIDO POLILÁCTICO
2011; Industrial University of Santander; Volume: 24; Issue: 1 Linguagem: Espanhol
ISSN
2145-8480
AutoresLeidy Marcela Gelves Jerez, Nerly Deyanira Montañez Supelano, Yurley Karina Anaya Jaimes, Hugo Armando Estupiñán Durán, Darío Yesid Peña Ballesteros, Custodio Vásquez Quintero, Dionisio A. Laverde C,
Tópico(s)Collagen: Extraction and Characterization
ResumoResumen En este trabajo se ha realizado una activacion superficial mediante irradiacion con luz UV, en peliculas de Acido Poli-Lactico (PLA), depositadas sobre cristales de cuarzo Au/Cr sobre la cual se estudia la adhesion y direccionamiento de proteinas de colageno y albumina bovina (BSA), bajo la imposicion de un sobrepotencial electroquimico anodico, hallado mediante voltametria ciclica, el cual garantiza una condicion de hidratacion y adsorcion de la proteina. Cambios de masa, de la capacitancia interfacial y de la impedancia de adsorcion de la monocapa proteinica, fueron evaluados mediante microbalanza de cristal de cuarzo (QCM) y Espectroscopia de Impedancia Electroquimica (EIS). Variaciones en la temperatura y en las concentraciones de las proteinas, fueron realizadas, para obtener parametros termodinamicos de adsorcion. Se planteo un modelo de circuito equivalente que muestra la adhesion de proteina preferencialmente direccionada sobre la superficie irradiada. Para verificar los resultados y los cambios obtenidos, se caracterizo la superficie empleando microscopia optica y FT-IR. Palabras clave: colageno, BSA, adsorcion, Gibbs, Langmuir. Abstract A superficial activation was made with the use of UV irradiation on Poly-lactic acid films (PLA) that were deposited on quartz crystal (Au/Cr). These are used to study the adhesion, and orientation of collagen, and bovine serum albumin (BSA) proteins under imposition of an electrochemical overpotential of anodic polarization and to be analyzed by cyclic voltammetry, which guarantees a condition of moisture and adsorption of the protein. Mass change of interfacial capacitance and impedance of adsorption of the monolayer protein was assessed using quartz crystal microbalance (QCM) and electrochemical impedance spectroscopy. Variations in temperature and concentrations of proteins were carried out to obtain thermodynamic parameters of adsorption. An equivalent circuit model was proposed which illustrated the preferential adhesion of protein directed towards the irradiated surface. To verify the results and changes, the surface was characterized with the use of optical microscopy and FT-IR. Keywords: collagen, BSA, adsorption, Gibbs, Langmuir.
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