期刊
EXPERIMENTAL CELL RESEARCH
卷 299, 期 2, 页码 335-342出版社
ELSEVIER INC
DOI: 10.1016/j.yexcr.2004.05.022
关键词
collagen fibrils; force-elongation profile; atomic force spectroscopy
资金
- NHLBI NIH HHS [HL07194-29] Funding Source: Medline
- NIAMS NIH HHS [1R01AR48195-01] Funding Source: Medline
In the field of biomechanics, collagen fibrils are believed to be robust mechanical structures characterized by a low extensibility. Until very recently, information on the mechanical properties of collagen fibrils could only be derived from ensemble measurements performed on complete tissues such as bone, skin, and tendon. Here, we measure force-elongation/relaxation profiles of single collagen fibrils using atomic force microscopy (AFM)-based force spectroscopy (FS). The elongation profiles show that in vitro-assembled human type I collagen fibrils are characterized by a large extensibility. Numerous discontinuities and a plateau in the force profile indicate major reorganization occurring within the fibrils in the 1.5- to 4.5-nN range. Our study demonstrates that newly assembled collagen fibrils are robust structures with a significant reserve of elasticity that could play a determinant role in the extracellular matrix (ECM) remodeling associated with tissue growth and morphogenesis. (C) 2004 Elsevier Inc. All rights reserved.
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