Unraveling the mechanics of collagen

Collagen is the predominant structural protein in humans, representing over 25% of protein mass in our bodies. Its unique triple-helical structure has the ability to assemble into biomechanically important, higher-order structures, such as the extracellular matrix and connective tissues including tendon. How amino-acid sequence prescribes local mechanics of collagen is not known, yet is key for understanding mechanobiological signalling and remodelling of strained and damaged tissues. We are investigating this link between sequence and mechanics, using atomic force microscopy (AFM) imaging of collagens and centrifuge force microscopy (CFM) for high-throughput force measurements. In this talk, I’ll present our first mapping of sequence to mechanics, and share insight into how this might influence the properties driving self-assembly of collagens into higher-order structures. I’ll also highlight the importance of environmental conditions on collagen’s mechanics and stability at the single-molecule level.