Structural investigations on native collagen type I fibrils using AFM.
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.
Strasser
Stefan
S
Department of Geo- and Environmental Sciences, Ludwig-Maximilians-Universität, 80333 Munich, Germany.
Zink
Albert
A
Janko
Marek
M
Heckl
Wolfgang M
WM
Thalhammer
Stefan
S
D024042:Collagen Type I / Q000737:chemistry* / Q000648:ultrastructure*; D003198:Computer Simulation; D004548:Elasticity; D006245:Hardness Tests; D042282:Microdissection / Q000379:methods*; D008846:Micromanipulation / Q000379:methods*; D018625:Microscopy, Atomic Force / Q000379:methods*; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D013314:Stress, Mechanical
D024042:Collagen Type I