Interactions between collagen IX and biglycan measured by atomic force microscopy

Chia Hsin Chen, Ming Long Yeh, Mark Geyer, Gwo Jaw Wang, Mao Hsiung Huang, Michael H. Heggeness, Magnus Hook, Zong Ping Luo

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


The stability of the lattice-like type II collagen architecture of articular cartilage is paramount to its optimal function. Such stability not only depends on the rigidity of collagen fibrils themselves, but more importantly, on their interconnections. One known interconnection is through type IX and biglycan molecules. However, the mechanical properties of this interaction and its role in the overall stability remain unrevealed. Using atomic force microscopy, this study directly measured the mechanical strength (or the rupture force) of a single bond between collagen IX and biglycan. The results demonstrated that the rupture force of this single bond was 15 pN, which was significantly smaller than those of other known molecule interactions to date. This result suggested that type IX collagen and biglycan interaction may be the weak link in the cartilage collagen architecture, vulnerable to abnormal joint force and associated with disorders such as osteoarthritis.

Original languageEnglish (US)
Pages (from-to)204-208
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Jan 6 2006


  • Atomic force microscopy
  • Biglycan
  • Binding force
  • Collagen IX

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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