Orientation distribution of highly oriented type I collagen deposited on flat samples with different geometries

Langmuir. 2013 Jun 4;29(22):6680-6. doi: 10.1021/la401421h. Epub 2013 May 17.

Abstract

The structural arrangement of type I collagen in vivo is critical for the normal functioning of tissues, such as bone, cornea, tendons, and blood vessels. At present, there are no established low-cost techniques for fabricating aligned collagen structures for applications in regenerative medicine. Here, we report on a straightforward approach to fabricate collagen films, with defined orientation distributions of collagen fibrillar aggregates within a matrix of oriented collagen molecules on flat sample surfaces. Langmuir-Blodgett (LB) technology was used to deposit thin films of oriented type I collagen onto flat substrates exhibiting various shapes. By varying the shapes of the substrates (e.g., rectangles, squares, circles, parallelograms, and various shaped triangles) as well as their sizes, a systematic study on collagen alignment patterns was conducted. It was found that the orientation and the orientation distribution of collagen along these various shaped substrates are directly depending on the geometry of the substrate and the dipping direction of that sample with respect to the collagen/water subphase. An important factor in tissue engineering is the stability, durability, and endurance of the constructed artificial tissue and thus its functioning in regenerative medicine applications. By testing these criteria, we found that the coated films and their alignments were stable for at least three months under different conditions and, moreover, that these films can withstand temperatures of up to 60 °C for a short time. Therefore, these constructs may have widespread applicability in the engineering of collagen-rich tissues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Collagen Type I / chemistry*
  • Glass / chemistry*
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Protein Stability
  • Surface Properties
  • Tissue Engineering / methods*

Substances

  • Collagen Type I