期刊
BIOMECHANICS AND MODELING IN MECHANOBIOLOGY
卷 12, 期 2, 页码 291-300出版社
SPRINGER HEIDELBERG
DOI: 10.1007/s10237-012-0399-2
关键词
Collagen; ECM (extracellular matrix); Mechanical test; Enzymatic degradation
资金
- NSF IGERT Nanomedicine Award [DGE-0504331]
- NIH [NEI-R01015500]
It has been established that the enzyme susceptibility of collagen, the predominant load-bearing protein in vertebrates, is altered by applied tension. However, whether tensile force increases or decreases the susceptibility to enzyme is a matter of contention. It is critical to establish a definitive understanding of the direction and magnitude of the force versus catalysis rate (k (C) ) relationship if we are to properly interpret connective tissue development, growth, remodeling, repair, and degeneration. In this investigation, we examine collagen/enzyme mechanochemistry at the smallest scale structurally relevant to connective tissue: the native collagen fibril. A single-fibril mechanochemical erosion assay with nN force resolution was developed which permits detection of the loss of a few layers of monomer from the fibril surface. Native type I fibrils (bovine) held at three levels of tension were exposed to Clostridium histolyticum collagenase A. Fibrils held at zero-load failed rapidly and consistently (20 min) while fibrils at 1.8 pN/monomer failed more slowly (35-55 min). Strikingly, fibrils at 23.9 pN/monomer did not exhibit detectable degradation. The extracted force versus k (C) data were combined with previous single-molecule results to produce a master curve which suggests that collagen degradation is governed by an extremely sensitive mechanochemical switch.
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