Department of Physics & Astronomy
University of New Mexico

Computational Physics Seminar

A chink in the armor: Dynamic structural defects in fibrillar collagen enable collagenase degradation

Presented by Keir C. Neuman, National Heart, Lung, and Blood Institute, National Institutes of Health

Collagen is the main component of the extracellular matrix. Fibrillar collagen is resistant to proteolysis and is degraded by specific matrix metalloproteases (MMPs). The process of fibrillar collagen degradation remains poorly understood. We observed collagen degradation by tracking individual MMPs engaged with native collagen fibrils. MMPs undergo one-dimensional biased and hindered diffusion interrupted by pauses periodically arrayed at ~1 µm intervals. MMPs initiate proteolysis at these pause sites. Remarkably, the pause sites exhibit collective motion that preserves the periodicity but not the phase of the pause pattern. The dynamic nature of the binding sites suggests that they correspond to transient structural defects in the collagen fibril. We propose that internal strain energy in fibrillar collagen is relieved by the formation of dynamic local defects that are periodically distributed along its length. We present a model that rationalizes these observations and provides a mechanistic paradigm for fibrillar collagen degradation.

1:30 pm, Friday, December 1, 2017
PAIS-2540, PAIS

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