Initial exploration of a fribronectin-collagen binding domain-derived fragment: integrating in silico and experimental methods for simulation and structural analysis
Valentine Albaret1, Thaddée Fassier1, Théana Fassier1, Julie Klein1, Manon Pizzinato1, Amina Ben Abla1, Jad Eid1
1École de Biologie Industrielle, EBInnov, 49 avenue des Genottes, 95895 Cergy-Pontoise, France
Abstract: Collagen and fibronectin (FN) are two abundant and essential macromolecules of the extracellular matrix. They interact directly with cells, modulating their adhesion and migration. This interaction is of interest to tissue engineering, aiming to develop biomimetic scaffolds for in vitro tissue reconstruction. Several protein chimeras carrying collagen-binding domains and cell-binding sites have been developed in our laboratory. These constructs have been genetically engineered and cell binding has already been validated. However, questions remain concerning the affinity interaction of the collagen-chimeric complex and the possible conformations of collagen in this chimera. In this project, we produced the chimeric protein and performed the collagen-binding assay. Several bioinformatics tools were used to predict the three-dimensional structure of the chimera in order to study collagen conformations in the chimera. To the best of our knowledge, we were the first to predict the three-dimensional structure of the chimera and showed that the collagen binding sites are well exposed. The chimera was successfully produced, and the results between the bioinformatics and experimental assays illustrate the strong affinity between collagen and chimera. Moving forward, it is imperative to incorporate additional in silico approaches to further validate such findings and enhance the understanding of the collagen-chimeric complex interaction.
Keywords: collagen, fibronectin, bioinformatics, protein-protein interaction, docking.