Self-association of type I collagen directed by thymoquinone through alteration of molecular forces.

Type I collagen is a vital structural component of the extracellular matrix providing the connective tissues with biomechanical support. One of the interesting properties of collagen is to self-associate into fibrils. The present work aims to direct the self-assembly of collagen through different molecular forces, which are tuned on the addition of thymoquinone a well-known phytochemical. A change in relative viscosity and stress of collagen-thymoquinone blends influenced the interfibrillar aggregates around its hydration shell. Further, secondary structural integrity was studied via cotton curve effect, and vibrational frequency shifts showed a characteristic interaction of thymoquinone at the N-terminal residues of the triple helix. Finally, the spontaneous self-association of fibrils was tracked by calculating the rate of fibril growth kinetics, which potentially decreased with increase in thymoquinone concentration. The fibrils were eventually visualized under the high resolution-scanning microscope showing morphological variations. Therefore, such a protein-phytochemical interaction may tend to play with the hydration network of collagen and covalently interact with its imino acid residues. It may be speculated that such an inhibitory process portrayed by thymoquinone may have a fortune in the targeted and sustainable delivery to the site of action for certain diseases, which includes collagen accumulation. Moreover, its directed assembly could be utilized for designing templates as in manipulating the collagen as a nanoporous membrane to make nanofibers and further tuned by small molecules for nanoparticle synthesis application.