Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1590177 | Micron | 2007 | 9 Pages |
Abstract
Colloidal gold labelling of the characteristic D-banded collagen type I fibrils with 5Â nm and 2Â nm chemically reactive gold particles reveals a periodic labelling pattern, which is not apparent with 10Â nm and 15Â nm gold particles, due to steric hindrance. The flexuous and spindle-shaped collagen fibrils also bind 2Â nm gold particles in a specific manner. In all cases, the specific chemisorption of gold onto the collagen fibrils is probably determined by the availability of repeating amino acid side chains of the collagen molecules along the fibril surface. The controlled production of varying stable collagen type I fibrillogenesis products is likely to be of value within numerous areas of biotechnology, biology and medicine, including experimental biomineralization.
Related Topics
Physical Sciences and Engineering
Materials Science
Materials Science (General)
Authors
J. Robin Harris, Andreas Reiber,