Communication

Temporal Assembly of Collagen Type II Studied by Atomic Force Microscopy†

  1. M. Dong1,
  2. S. Xu1,
  3. M. H. Bünger2,
  4. H. Birkedal3,
  5. F. Besenbacher1

Article first published online: 19 DEC 2007

DOI: 10.1002/adem.200700220

Issue

Advanced Engineering Materials

Advanced Engineering Materials

Special Issue: Biomaterials

Volume 9, Issue 12, pages 1129–1133, December, 2007

Additional Information

How to Cite

Dong, M., Xu, S., Bünger, M. H., Birkedal, H. and Besenbacher, F. (2007), Temporal Assembly of Collagen Type II Studied by Atomic Force Microscopy. Adv. Eng. Mater., 9: 1129–1133. doi: 10.1002/adem.200700220

Author Information

  1. 1

    Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, Department of Physics and Astronomy &

  2. 2

    Department of Endocrinology and Metabolism C, Aarhus University Hospital

  3. 3

    Department of Chemistry, Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, DK-8000 Aarhus C, Denmark

  1. †

    We are grateful to the valuable suggestions from Prof. Peter Hinterdorfer of University of Linz in Austria. We acknowledge financial support from the Danish Ministry of Science, Technology and Innovation through the iNANO center and the Danish Research Council through the “Large Interdisciplinary Research Group – Nanoscience & Biocompatibility” (2052-01-0006). HB thanks the Danish Natural Science Research Council and the Danish Research Council for Production and Technology Sciences for support through a Steno research assistant professorship.

Publication History

  1. Issue published online: 19 DEC 2007
  2. Article first published online: 19 DEC 2007

Funded by

  • Danish Ministry of Science, Technology and Innovation
  • Danish Research Council through the “Large Interdisciplinary Research Group – Nanoscience & Biocompatibility” . Grant Number: (2052-01-0006)
  • Danish Natural Science Research Council
  • Danish Research Council for Production and Technology Sciences

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Keywords:

  • AFM;
  • Fibrillogenesis;
  • Self-assembly
Thumbnail image of graphical abstract

The hierarchical self-assembly of collagen type II, the major fibril-forming collagen of cartilage, has been studied by atomic force microscopy (AFM). The fibrillation of human collagen type II in simulated body fluid (SBF) was investigated by varying the incubation time, pH, and temperature as well as the collagen concentration. The results reveal that the collagen type II fibrillogenesis process from procollagen into D-banded fibrils is entropy driven, and that incubation at low temperature leads to the formation of distinct hierarchical supramolecular assemblies.

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