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Center for Astrophysics Research and Technologies Seminar Series Information

 

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

Friday December 1, 2017
1:30 pm


 Presenter:  Keir C. Neuman,
National Heart, Lung, and Blood Institute, National Institutes of Health
 Series:  Physics Seminars
 Abstract:  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 ┬Ám 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.
 Host:  Keith Lidke
 Location:  Room 190, Physics & Astronomy

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