Your browser doesn't support javascript.
loading
Electron Transport in Muscle Protein Collagen.
Kolay, Jayeeta; Bera, Sudipta; Mukhopadhyay, Rupa.
Afiliación
  • Kolay J; School of Biological Sciences , Indian Association for the Cultivation of Science , Jadavpur , Kolkata 700 032 , India.
  • Bera S; School of Biological Sciences , Indian Association for the Cultivation of Science , Jadavpur , Kolkata 700 032 , India.
  • Mukhopadhyay R; School of Biological Sciences , Indian Association for the Cultivation of Science , Jadavpur , Kolkata 700 032 , India.
Langmuir ; 35(36): 11950-11957, 2019 09 10.
Article en En | MEDLINE | ID: mdl-31404493
ABSTRACT
In recent times, collagen, which is one of the most abundant proteins in animals, has appeared to be an attractive candidate for biomaterial applications, for example, in medical implants and wearable electronics. This is because collagen is water-insoluble, biocompatible, and nontoxic. In addition, films of different sizes and shapes can be made using this protein as it is malleable and elastic in nature. However, its electron transport capacity or its absence has remained largely untested so far. Therefore, in this work, the electron transport behavior of collagen has been studied in both film and single-fiber states in a local probe configuration using current-sensing atomic force spectroscopy (CSAFS). From the CSAFS analyses, the electronic (transport) band gap of collagen has been estimated. It has been found that collagen behaves as a wide band gap semiconductor (near-insulating) in a variety of experimental conditions. The transition to a semiconducting material with a low electronic band gap and a nearly 1000-fold enhancement of current (picoampere to nanoampere level) occurs by metal ion treatment (here, Fe3+) of the native collagen. To the best of our knowledge, this is the first report of a molecular level study of the electron transport behavior of collagen proteins and estimation of transport band gap values of collagen and metalated collagen.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Colágeno / Proteínas Musculares Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2019 Tipo del documento: Article País de afiliación: India

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Colágeno / Proteínas Musculares Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2019 Tipo del documento: Article País de afiliación: India