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Highly sensitive single-fibril erosion assay demonstrates mechanochemical switch in native collagen fibrils

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An Erratum to this article was published on 04 June 2013

Abstract

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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Authors and Affiliations

  1. Department of Mechanical and Industrial Engineering, Northeastern University, Boston, MA, 02115, USA

    Brendan P. Flynn, Graham E. Tilburey & Jeffrey W. Ruberti

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  1. Brendan P. Flynn
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  2. Graham E. Tilburey
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  3. Jeffrey W. Ruberti
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Correspondence to Jeffrey W. Ruberti.

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Flynn, B.P., Tilburey, G.E. & Ruberti, J.W. Highly sensitive single-fibril erosion assay demonstrates mechanochemical switch in native collagen fibrils. Biomech Model Mechanobiol 12, 291–300 (2013). https://doi.org/10.1007/s10237-012-0399-2

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