Collagen is the most abundant protein found in human tissues such as tendon and skin. Fundamental understanding regarding both molecular assembly processes and resultant structural features of collagen helps toward eventual synthetic replication of this bio-material. To date, wide arrays of research studies have been performed to synthetically process and replicate collagen materials. Several of these studies have shown evidence of collagen mimicry. However, synthetic replication of collagen assembly from the molecular to macroscopic level (i.e., fiber) remains a challenge, especially in comparison to native fibrous tissues like tendon and skin. In this study a gel-based fibril/fiber assembly process has been developed, where truly mimetic synthetic collagen structures was successfully made. This self-assembly process relies critically on many processing factors, such as temperature, PH, ionic strength, as well as gelation time and aging. What is unique in regards to this processing approach is the ability to tune the micro-environmental conditions to capture and understand each level of structural hierarchy involved as the collagen molecular assembles into a fibril/fiber form. Structural evolution was tracked and analyzed by several characterization approaches including scanning electron microscopy (SEM), atomic force microscopy (AFM) and small-angle X-ray scattering (SAXS), which help to reveal growth and development mechanisms. In addition to molecular stacking, a nano to microscopic braiding/twisting mechanism is also found to play a key role in the formation of fibril growth and morphology. These results are outlined in this work and provide insight about collagen self-assembly processes, and may also provide insight to help build synthetic biopolymer-based materials with complex structures for engineered tissues.

Synthetic control of molecular-to-macroscopic collagen assembly and structural mimicry

251st National Meeting (2016)

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