Collagen triple helix (CTH) (CTH)

The collagen triple helix is the fundamental structural unit of collagen, characterized by three polypeptide alpha-chains coiled into a right-handed superhelix (Shoulders & Raines, 2009). This motif is defined by a repeating Gly-X-Y sequence, where glycine's small size allows for tight packing and hydrogen bonding provides stability (Brodsky & Persikov, 2005). Biologically, it provides tensile strength to the extracellular matrix (ECM) and regulates cell behavior through interactions with integrins and other receptors (Ricard-Blum, 2011). In diseases such as fibrosis and scleroderma, excessive deposition of the triple helix leads to organ dysfunction, while mutations in the helical domain cause disorders like Osteogenesis Imperfecta (Deshmukh et al., 2016). Therapeutic targeting involves enzymatic degradation using Collagenase clostridium histolyticum for conditions like Dupuytren's contracture (Hurst et al., 2009). Additionally, Collagen-hybridizing peptides (CHPs) are being developed to target denatured triple helices for imaging and drug delivery in cancer and arthritis (Li & Yu, 2013).

Other names

TropocollagenCollagen helixTriple-helical domainCollagen type I triple helixCollagen type III triple helix

Enzymatic proteolysis of the triple helical domain to dissolve pathological collagen deposits (Hurst et al., 2009); hybridization with denatured collagen strands for targeted delivery and imaging (Li & Yu, 2013).