Films of collagen crosslinked by S–S bonds: preparation and characterization

Collagen (type I from calf-skin) was chemically modified by 4-butyrothiolactone to obtain the mercapto group-bearing collagen (collagenSH), which possessed SH groups in 8–19 M% of a total amino acid residues. The triple helical strands of the collagen was not completely perturbed to exhibit the rotary dispersion [θ]221, which was as much as 70% of an original intensity of the collagen. In the presence of the oxygen dissolved in water, the collagenSH was cross-linked by disulfide bonds to afford the collagenSS. The collagenSS could preserve about 15 and 40% of an original helix structure at 55–70°C and in 2 mm sodium dodecyl sulfate, respectively. The film made of the collagenSS exhibited the tensile strength as high as 36 MPa and was insoluble in most organic solvents including water. The collagenSS film was more resistant to degradation by collagenase (type I) than the collagen film. The collagenSS film supported the growth of L929 fibroblast cell in a manner similar to a collagen film.