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Open Access Green as soon as Postprint is submitted to ZB.
Structural investigations on native collagen type I fibrils using AFM.
Biochem. Biophys. Res. Commun. 354, 27-32 (2007)
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.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
AFM; microdissection; force spectroscopy; collagen
ISSN (print) / ISBN
0006-291X
e-ISSN
1090-2104
Quellenangaben
Volume: 354,
Issue: 1,
Pages: 27-32
Publisher
Elsevier
Reviewing status
Peer reviewed
Institute(s)
Institute of Radiation Protection (ISS)