The organization of cross-linking in collagen fibrils

The cross-linked peptides in cyanogen bromide digests from rabbit and calf fibrils of type I collagen have been compared by gel filtration and electrophoresis. Fibrils were prepared in vitro from acid-soluble collagen, or tendons were used; both were reduced with borohydride to stabilize cross-linking adducts. The cross-linked peptides were isolated and hydrolyzed, and the reducible cross-links were analyzed. We propose that a prominent pattern of cross-linking involves in-register palisades of molecules overlapping by 27 nm and joined through the condensation of amino-terminal aldol adducts on the carboxy-terminal helical regions of overlapping molecules. Lateral association probably occurs through the carboxy-terminal aldehydes from two molecules forming tri- or quadrivalent adducts with residues in the overlapped molecule. This model favors the recently proposed quasi-hexagonal organization of molecules in fibrils in which rows of molecules occur in lateral register.