A role for disulphide bridges in the protein core in the interaction of proteodermatan sulphate and collagen.
Proteodermatan sulphate from bovine skin retarded precipitation of fibrils from solutions of purified acid-soluble bovine skin collagen. The isolated protein core was as effective as the intact proteoglycan. Thermal denaturation leading to almost complete loss of the native secondary structure, (determined by circular dichroism spectroscopy to consist of about 60% beta structure) did not diminish the effect unless accompanied by reduction of disulphides, of which there were shown to be three per molecule. The reduced and alkylated protein core was totally ineffective. Electron-microscopy revealed a D-periodic arrangement of glycosaminoglycan on the surfaces of collagen fibrils precipitated in the presence of proteodermatan sulphate. Dermatan sulphate (with attached small peptide) prepared from the proteoglycan, had no effect on the rate of fibrillogenesis and was apparently not bound to the fibrils.
D000818:Animals; D002417:Cattle; D002807:Chondroitin / Q000031:analogs & derivatives*; D002942:Circular Dichroism; D003094:Collagen / Q000378:metabolism*; D003871:Dermatan Sulfate / Q000378:metabolism*; D004220:Disulfides; D046911:Macromolecular Substances; D011485:Protein Binding; D011487:Protein Conformation; D011509:Proteoglycans / Q000378:metabolism*; D013329:Structure-Activity Relationship
D004220:Disulfides; D046911:Macromolecular Substances; D011509:Proteoglycans; D003871:Dermatan Sulfate; D002807:Chondroitin; D003094:Collagen