Biomolecular Principles of Matrix Assembly Related to Fracture Resistance
Abstract
One of the major engineering feats of the developing spicule matrix is the assembly of a protein scaffolding network that readily adapts itself to the emergence of ACC clusters and eventually persists within an intracrystalline environment as the ACC phase transforms into crystalline calcite. Collectively, our findings indicate that SM50 is suitably adapted for a major role in this process. We confirm that rSM50 spontaneously oligomerizes to form amorphous, heterogeneous supramolecular protein complexes that can form films and behave in a relatively mobile fashion. This would provide a means for quickly assembling a protein matrix with fluid or labile features that are commensurate with those of the ACC phase itself. Moreover, the lability of rSM50 assemblies would provide an adaptation to the changing shape and dimension of spicules as they undergo developmental elongation and maturation, i.e., the SM50-dominated spicule matrix would be plastic for all intents and purposes and thus is perfectly suited for embryonic development and eventual mineralization, with the added benefit of providing a cushioning or compressive phase as fracture-resistant intracrystalline components within crystalline calcite.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 24, 2013
- Accession Number
- ADA600953
Entities
People
- John S. Evans
Organizations
- New York University