Collagen triple helix

The **collagen triple helix** is a structural motif formed by the association of three polypeptide chains with a Gly–Xaa–Yaa repeating triplet pattern, where proline and 4-hydroxyproline are common in Xaa and Yaa positions, respectively[1][2][4]. The triple helix is stabilized by interchain hydrogen bonds, water-mediated networks, and specific stereoelectronic effects, particularly from 4-hydroxyproline residues[2][4]. Formation and stabilization of this structure are critical for functional collagen fibers, which provide structural support and integrity to the extracellular matrix of connective tissues[1][2][3]. Disruptions—due to genetic mutations or altered post-translational modifications—can result in various connective tissue diseases, including osteogenesis imperfecta and Ehlers-Danlos syndromes[4]. The triple helix itself is not a single molecule, receptor, or enzyme, but rather a motif or conformation shared by all collagen proteins; therefore, it is not directly druggable as a therapeutic target, though stabilization strategies are studied in peptide engineering and regenerative medicine for modulating collagen stability[2][3][5].

Other names

Collagen triple-helical regionCollagen triple helix domainTriple-helical collagen