Published Paper Details:

Collagen serves as both scaffold and signal in mammalian tissues, providing tensile strength while encoding biochemical cues in its triple helical sequence. A central question in matrix biology is how cells convert this motif level information into adhesion, migration, differentiation, and repair. In skin and many soft tissues, fibrillar collagens I and III dominate the mechanical landscape; cells interpret these fibers largely through collagen binding integrins (?1?1, ?2?1, ?10?1, ?11?1) and the discoidin domain receptors DDR1/DDR2. Systematic Collagen Toolkits devised in Richard Farndale's laboratory (University of Cambridge) mapped short triple helical peptides and defined key motifs - GFOGER/GxOGER for integrin ?2?1 and related ?I containing integrins, GLOGEN/GROGER for ?1?1 preference, and GVMGFO for DDRs, thus revealing how cells "read" collagen at amino acid resolution. Integrating structural, biochemical, and functional data, this review synthesizes how fibroblasts, keratinocytes, endothelial cells, chondrocytes, immune cells, and platelets use these receptors to extract meaning from collagen, with special attention to the HUVEC study by Hunter et al. (2022) that disentangles integrin usage during adhesion, migration, and tube formation on collagen. Finally, I discuss how motif aware insights now inform biomaterial design, wound care, dermatology, and aesthetics, where engaging or modulating specific collagen-receptor axes may improve outcomes.