Internal strain drives spontaneous periodic buckling in collagen and regulates remodeling

Andrew Dittmore, Jonathan Silver, Susanta K. Sarkar, Barry Marmer, Gregory I. Goldberg, Keir C. Neuman

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


Fibrillar collagen, an essential structural component of the extracellular matrix, is remarkably resistant to proteolysis, requiring specialized matrix metalloproteinases (MMPs) to initiate its remodeling. In the context of native fibrils, remodeling is poorly understood; MMPs have limited access to cleavage sites and are inhibited by tension on the fibril. Here, single-molecule recordings of fluorescently labeled MMPs reveal cleavage-vulnerable binding regions arrayed periodically at ∼1-μm intervals along collagen fibrils. Binding regions remain periodic even as they migrate on the fibril, indicating a collective process of thermally activated and self-healing defect formation. An internal strain relief model involving reversible structural rearrangements quantitatively reproduces the observed spatial patterning and fluctuations of defects and provides a mechanism for tension-dependent stabilization of fibrillar collagen. This work identifies internal-strain-driven defects that may have general and widespread regulatory functions in selfassembled biological filaments.

Original languageEnglish
Pages (from-to)8436-8441
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number30
StatePublished - Jul 26 2016


  • Collagenase
  • Matrix metalloproteinase
  • Mechanosensing
  • Pattern formation
  • Single molecule


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