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Molecular simulations predict novel collagen conformations during cross-link loading.

Jonathan W Bourne1, Peter A Torzilli

  • 1Physiology, Biophysics & Systems Biology Program, Weill Graduate School of Medical Sciences, Cornell University, 1300 York Avenue, New York, NY 10065, USA. BourneJ@HSS.EDU

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Collagen cross-links strengthen tissues, but how force affects their structure is unclear. Molecular dynamics show collagen disrupts its helix shape under force before breaking, revealing new molecular conformations during mechanical stress.

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Area of Science:

  • Biophysics
  • Materials Science
  • Molecular Biology

Background:

  • Collagen cross-linking is crucial for tissue mechanical strength throughout life.
  • Limited understanding exists on how forces at cross-links influence collagen's molecular structure.

Purpose of the Study:

  • To investigate the effect of mechanical force on collagen molecular conformation.
  • To model the transmission of force across collagen cross-links.

Main Methods:

  • Steered Molecular Dynamics (SMD) simulations were employed.
  • Perpendicular force was modeled acting through a collagen side chain.

Main Results:

  • Collagen peptides exhibit minimal resistance to bending.
  • Mechanical force induces collagen helix disruption at forces below covalent bond failure.
  • This suggests structural changes occur before cross-link rupture.

Conclusions:

  • Collagen molecular conformation changes significantly under mechanical load.
  • Alternative conformations may precede macroscopic tissue damage and cross-link failure.