Effect of molecular chirality on the collagen self-assembly

Chirality is a basic property of nature and plays an important role in several biological activities of living organisms. However, the function of chirality in the self-assembly of natural collagen is still unclear. Herein, we investigated the effect of chirality on the self-assembly of bovine Achilles tendon collagen (BATC) using d/l-glutamic acid (GA) as model molecules. Kinetic studies indicated that the rate of self-assembly of d-GA/BATC was faster than that of l-GA/BATC. Results from scanning electron microscopy showed that collagen fibrils assembled in the presence of l-GA had a larger diameter than those assembled in the presence of d-GA. Differential scanning calorimetry and viscoelasticity analyses confirmed that l-GA/BATC gel had better thermal stability and mobility than the corresponding d-GA/BATC gel. Collectively, these results indicated that molecular chirality can be used as a novel strategy to regulate the performance of collagen self-assembly products.