Attachment and conformational changes of collagen on bioactive glass surface

Biomed Mater Eng. 2016 May 12;27(1):63-74. doi: 10.3233/BME-161567.

Abstract

The proteins adsorption on biomaterials surface leads to changes in their structural conformation that may further influence the adhesion, migration and growth of cells. The aim of this study was to examine the attachment of collagen (calf skin type I) on bioactive glass powders and the conformational changes of the protein. Scanning electron microscopy analysis and X-ray photoelectron spectroscopy measurements indicate that the collagen cover the glass surface in a nanometric thin layer. The infrared amide I absorption signal shows pronounced changes in the secondary structure of the adsorbed collagen.

Keywords: Collagen; FT-IR; SEM; XPS; adsorption.

MeSH terms

  • Adsorption
  • Animals
  • Biocompatible Materials / chemistry
  • Cattle
  • Collagen Type I / chemistry*
  • Collagen Type I / ultrastructure
  • Glass / chemistry
  • Microscopy, Electron, Scanning
  • Protein Conformation
  • Spectroscopy, Fourier Transform Infrared
  • Surface Properties

Substances

  • Biocompatible Materials
  • Collagen Type I