Probing elastin molecules and networks using holographic optical tweezers

Astrid van der Horst
Simon Fraser University

Elastin is a major extracellular matrix protein in, e.g., our arteries and skin, where it provides 
extensibility and elasticity. Synthesized as a monomer (~200 nm long), elastin self-assemble into 
ordered fibrillar structures with remarkable elasticity, and once laid down during development it 
does not turn over appreciably, lasting us a lifetime. Uncovering the molecular basis of the unusual 
elastomeric properties and self-assembly of elastin will give insight into its physiological 
functioning. In addition, it will supply useful principles for designing elastin-based biomaterials.  
Using recombinant elastin-like polypeptides (ELPs), of which the peptide sequence can be varied at 
will, we will investigate the influence of certain naturally occurring human peptide domains on the 
elasticity and structure of elastin monomers, and the elastomeric properties of fibrils.  So far, 
elastin’s mechanical properties have mainly been investigated in macro-scale tensile experiments. 
Optical tweezers give unique and unprecedented experimental access to single-molecule wild type 
elastin and ELPs, and to self-assembled fibrillar structures on the micrometer-scale.  In my talk I 
will introduce the holographic optical tweezers setup I built in the Forde Lab for these proposed 
measurements, in addition to elaborate on what to date is known about elastin’s elasticity and 
self-assembly and the questions that are left.