Selwyn Yorke - Glycosaminoglycan specificity of a heparin-binding peptide

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      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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