Structural investigations on native collagen type I fibrils using AFM

Stefan Strasser, Albert Zink, Marek Janko, Wolfgang M. Heckl, Stefan Thalhammer

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94 Scopus citations

Abstract

This study was carried out to determine the elastic properties of single collagen type I fibrils with the use of atomic force microscopy (AFM). Native collagen fibrils were formed by self-assembly in vitro characterized with the AFM. To confirm the inner assembly of the collagen fibrils, the AFM was used as a microdissection tool. Native collagen type I fibrils were dissected and the inner core uncovered. To determine the elastic properties of collagen fibrils the tip of the AFM was used as a nanoindentor by recording force-displacement curves. Measurements were done on the outer shell and in the core of the fibril. The structural investigations revealed the banding of the shell also in the core of native collagen fibrils. Nanoindentation experiments showed the same Young's modulus on the shell as well as in the core of the investigated native collagen fibrils. In addition, the measurements indicate a higher adhesion in the core of the collagen fibrils compared to the shell.

Original languageEnglish
Pages (from-to)27-32
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume354
Issue number1
DOIs
StatePublished - 2 Mar 2007
Externally publishedYes

Keywords

  • AFM
  • Collagen
  • Force spectroscopy
  • Microdissection

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