Publication Details (including relevant citation information):
Peptide Research (1995), 8(5), 286-93
Glycosaminoglycans are complex sulfated polysaccharides with a diverse range of biol. functions. Three glycosaminoglycan stds. (chondroitin sulfate, dermatan sulfate and heparin) were characterized during this study. The interaction of the heparin binding site of protein C inhibitor, represented by the peptide sequence 264-283, in soln. with the above glycosaminoglycan stds. was studied. CD spectroscopy was used to det. the dominant secondary structure induced in the peptide upon binding the relevant glycosaminoglycans. The various glycosaminoglycans induced different secondary structures. The level of induced secondary structure by dermatan sulfate and heparin was approx. twice that induced by chondroitin sulfate. For chondroitin sulfate and heparin, .alpha.-helix was the dominant ordered secondary structure, whereas for dermatan sulfate the .beta.-strand conformation dominated. The order of secondary structure induction of the protein C inhibitor peptide by the glycosaminoglycans paralleled the reported biol. activities of these glycosaminoglycans for mediation of the biol. activity in the intact protein. The strength of the interaction of dermatan sulfate and heparin with the protein C inhibitor peptide was measured by detg. the concn. of salt required to inhibit 50% of the interaction. The values detd. were 0.1 and 0.3 M salt for dermatan sulfate and heparin, resp. These results show that different glycosaminoglycans can support different secondary structures in the protein C inhibitor peptide.
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