Collagen I

Collagen I is the predominant fibrillar collagen in the extracellular matrix and provides tensile strength, structural integrity, and mechanical support to bone, skin, tendon, ligament, and vascular tissues through the assembly of highly ordered collagen fibrils.[1][2] Type I collagen is composed of two α1(I) chains and one α2(I) chain that form a triple-helical procollagen molecule, which undergoes enzymatic processing and extracellular fibril formation to generate mature collagen fibers.[3][4] Mechanistically, collagen I regulates extracellular matrix organization and tissue architecture by forming stable cross-linked fibrillar networks that support cell adhesion, tissue repair, and connective tissue homeostasis.[1][3] In disease models, mutations affecting COL1A1 disrupt collagen assembly, fibrillogenesis, and matrix stability, leading to disorders including osteogenesis imperfecta and Ehlers-Danlos syndrome, highlighting the essential role of collagen I in skeletal and connective tissue integrity.[4] Compared with other collagen isoforms that form specialized extracellular matrix structures, collagen I is distinguished by its abundance and dominant contribution to fibrillar matrix formation in connective tissues.[1][2] For experimental applications, collagen I is widely used as a biomaterial and extracellular matrix model for investigating cell-matrix interactions, tissue remodeling, fibrosis, and regenerative processes because of its well-characterized fibrillar architecture and biomechanical properties.[1][2]