The aim of this research was to investigate the use of atomic force microscopy (AFM) for the high-resolution imaging of collagen fibers in aqueous media. Collagen plays a vital role in many processes in vivo, especially in structural integrity, yet few studies have used AFM to investigate the structure of these fibers. Type I collagen was used in this study on AP-mica, poly-L-lysine-coated glass slides and on ethanol-cleaned glass slides to determine what structures these fibers assume in vitro under the various conditions. It was found that AFM is in fact a viable method for determining collagen structure, and that type I fibrils can be seen in both cross-linked and isolated forms. A resolution of about 20–30 nm was achieved. This research forms a foundation for further investigation into the different types of collagen structures in vivo and the environmental conditions that cause them.

Last modified

• 07/17/2018

Creator

• Horacio Espinosa
• Yoshiro Fukui
• Keun-Ho Kim
• Isabel Nocedal

DOI

• https://doi.org/10.21985/N2TM6F

Keyword

• Volume 3

Date created

• 2006

Resource type

• Article

Rights statement

• In Copyright