Evidence for singlet oxygen-induced cross-links and aggregation of collagen.

Singlet oxygen, generated by a hematoporphyrin-photosensitized reaction, was shown to cause insolubilization and an increase in molecular weight of acid soluble type I collagen and vitreous collagen as manifested in sodium dodecyl sulfate polyacrylamide gel electrophoresis. No such changes in the molecular properties of collagen could be observed when the irradiation was carried out in the presence of sodium azide, a singlet oxygen quencher. The increase in molecular weight and insolubilization of the collagen solution was attributed to extensive cross-links in the protein molecules.