Mechanical properties of a collagen fibril under simulated degradation

David C. Malaspina, Igal Szleifer, Yasin Dhaher

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Collagen fibrils are a very important component in most of the connective tissue in humans. An important process associated with several physiological and pathological states is the degradation of collagen. Collagen degradation is usually mediated by enzymatic and non-enzymatic processes. In this work we use molecular dynamics simulations to study the influence of simulated degradation on the mechanical properties of the collagen fibril. We applied tensile stress to the collagen fiber at different stages of degradation. We compared the difference in the fibril mechanical priorities due the removal of enzymatic crosslink, surface degradation and volumetric degradation. As anticipated, our results indicated that, regardless of the degradation scenario, fibril mechanical properties is reduced. The type of degradation mechanism (crosslink, surface or volumetric) expressed differential effect on the change in the fibril stiffness. Our simulation results showed dramatic change in the fibril stiffness with a small amount of degradation. This suggests that the hierarchical structure of the fibril is a key component for the toughness and is very sensitive to changes in the organization of the fibril. The overall results are intended to provide a theoretical framework for the understanding the mechanical behavior of collagen fibrils under degradation.

Original languageEnglish (US)
Pages (from-to)549-557
Number of pages9
JournalJournal of the Mechanical Behavior of Biomedical Materials
Volume75
DOIs
StatePublished - Nov 2017
Externally publishedYes

Keywords

  • Collagen
  • Degradation
  • MMP
  • Molecular dynamics

ASJC Scopus subject areas

  • Biomaterials
  • Biomedical Engineering
  • Mechanics of Materials

Fingerprint Dive into the research topics of 'Mechanical properties of a collagen fibril under simulated degradation'. Together they form a unique fingerprint.

Cite this