Benzo[a]pyrene-collagen interactions

In vitro interactions of benzoa]pyrene (BaP) with acid-soluble type I collagen from rat tail tendon have been investigated. The fluorescence of BaP increases in the presence of collagen. Bound BaP inhibits the formation of collagen fibrils in solution. When BaP-collagen complexes are irradiated in air with UV (365 nm) light, BaP rapidly undergoes photooxidation with the further inhibition of fibril formation. Viscosity and circular dichroism (CD) studies show that neither BaP nor further UV-irradiation alters the size or helical conformation of the protein. During thermal denaturation of collagen, BaP fluorescence changes. Collagen from young rat tail tendon shows a pronounced drop at about 38 degrees C, whereas that from old rat tail tendon exhibits an increase with a plateau in the same temperature range. These anomalous changes are observed when tyrosine residues, present only in the non-helical terminal telopeptides of collagen, are excited at 275 nm, but not by direct BaP excitation at 387 nm. These findings suggest that the specific hydrophobic telopeptide region, which plays an important role in fibril formation, are affected by bound BaP.