Fiber Formation from Liquid Crystalline Collagen Vesicles Isolated from Mussels

Marine mussels (Mytilus edulis) fabricate byssal threads, high-performance biopolymeric fibers, which exhibit exceptional toughness and self-healing capacity. These properties are associated with collagenous proteins in the fibrous thread core known as preCols that self-organize into a hierarchical semicrystalline structure. Threads assemble individually in a bottom-up process lasting just minutes via secretion of membrane bound vesicles filled with preCols. However, very little is understood about the details and dynamics of this assembly process. Here, we explore the hypothesis that preCols are stored within the vesicles in a liquid crystalline phase, which contributes to fiber assembly by preordering molecules. To achieve this, a protocol was developed for extracting and isolating intact preCol secretory vesicles in high yield and purity. Vesicles were characterized and were manipulated in vitro, clearly indicating the dynamic liquid crystalline nature of the proteins within. Moreover, mechanical shearing of vesicles led to formation of highly birefringent preCol fibers. These findings have relevance for efforts toward sustainable production of advanced polymeric materials, and possibly for engineering biomedical scaffolds based on collagenous proteins.