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Interactions between mucopolysaccharides and cationic polypeptides in aqueous solution: Chondroitin 4‐sulfate and dermatan sulfate
Author(s) -
Gelman R. A.,
Blackwell J.
Publication year - 1973
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1973.360120904
Subject(s) - dermatan sulfate , chemistry , chondroitin , chondroitin sulfate , cationic polymerization , glycosaminoglycan , circular dichroism , sulfate , arginine , biochemistry , stereochemistry , amino acid , polymer chemistry , organic chemistry
Abstract Circular dichroism spectroscopy has been used to study the interactions of both dermatan sulfate and chondroitin 4‐sulfate with the cationic polypeptides; poly( L ‐arginine), poly( L ‐lysine), and poly( L ‐ornithine). The results indicate that the mucopolysaccharides have a conformation directing effect on both poly( L ‐arginine) and poly‐( L ‐lysine) such that these polypeptides adopt the α‐helical conformation. The extent of interaction in each polypeptide‐polysaccharide system can be judged by the degree of induced helicity and the “melting temperature” at which the interaction is disrupted On comparison of these results with those previously obtained for chondroitin 6‐sulfate‐polypeptide mixtures, the extent of interaction can be seen to depend on the length of the amino acid side chain and the positions of the anionic groups on the mucopolysaccharide chain. Such considerations place the three mucopolysaccharides in order of increasing interaction: chondroitin 4‐sulfate < chondroitin 6‐sulfate < dermatan sulfate. These results are correlated with observations that dermatan sulfate is bound more tightly to collagen in connective tissues than are the other two polysaccharides.