Extensible Collagen in Mussel Byssus: A Natural Block Copolymer

• DOI: 10.1126/science.277.5333.1830
• Publication Date: 2002-07-27T09:44:47Z
• Authors: Kathryn J. Coyne; Xiao-Xia Qin; J. Herbert Waite
• Keywords: 0301 basic medicine; Alanine; DNA, Complementary; Base Sequence; Proline; Protein Conformation; Molecular Sequence Data; Glycine; Elasticity; Protein Structure, Secondary; Bivalvia; Elastin; 03 medical and health sciences; Biopolymers; Serine; Animals; Histidine; Amino Acid Sequence; Collagen; Protein Precursors; Fibroins; Sequence Alignment

To adhere to solid surfaces, marine mussels produce byssal threads, each of which is a stiff tether at one end and a shock absorber with 160 percent extensibility at the other end. The elastic extensibility of proximal byssus is extraordinary given its construction of collagen and the limited extension (less than 10 percent) of most collagenous materials. From the complementary DNA, we deduced that the primary structure of a collagenous protein (preCol-P) predominating in the extensible proximal portion of the threads encodes an unprecedented natural block copolymer with three major domain types: a central collagen domain, flanking elastic domains, and histidine-rich terminal domains. The elastic domains have sequence motifs that strongly resemble those of elastin and the amorphous glycine-rich regions of spider silk fibroins. Byssal thread extensibility may be imparted by the elastic domains of preCol-P.