Abstract
Collagen, characterized by the unique triple helical structure, is a main component of the extracellular matrix, and exists in almost all parts of the body such as skin and bone. It is considered that denatured collagen, which has unfolded portions in the triple helical molecule, is produced and accumulated during the degradation process in the tissues surrounding malignant tumors. Collagen-mimetic peptide (CMP) is a generic name for chemically synthesized peptides that mimic the triple helical structure of collagen. A single-stranded CMP can hybridize to the loose triple helical parts of collagen by its inherent triple helix-forming propensity. In this review, we summarize studies on the collagen-hybridizing CMPs, and introduce a new DDS concept that targets changes in the structure of extracellular matrices. Although the relationship between collagen denaturation and diseases is not well understood, the collagen-hybridizing CMP would be useful for understanding of pathological conditions, and development of new diagnostic and therapeutic strategies.
