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Heparin/heparan sulfate (HS) interacts with numerous proteins, including various enzymes, growth factors, cytokines, and extracellular matrix proteins, etc. It is widely believed that most of their biological functions depend upon direct binding of the various functional proteins to the polysaccharide chains, mediated by specific domains with distinct saccharide sequences. For example, interaction of members of the FGF family with heparin/HS requires different combinations of sulfate groups, hence different saccharide sequences. On the other hand, several analyses of the structural features of many known heparin! HS-binding proteins have revealed the presence of conserved motifs, through which heparin/HS-binding has been postulated to occur. In a paper that has been widely cited, Cardin and Weintraub identified two clusters of basic charge in known heparin /HS-binding proteins in which amino acids tend to be arranged in the patterns, XBBXBX or XBBBXXBX, where B represents an amino acid with basic charge, usually arginine or lysine, and X represents an uncharged or hydrophobic amino acid [Cardin, A.D., and Weintraub, H.J.R. (1989) Arteriosclerosis 9, 21-32]. Molecular modeling of these consensus sites predicts the arrangement of amino acids into either ƒ¿-helices ƒÀ-strands. This allows for the clustering of noncontiguous basic amino acids on one side of the helix, thus forming a charged domain to which heparin/HS could bind. Indeed, for some but not all of the heparin-binding proteins, disruption of the consensus sequences hinders its heparinlHS-binding. The authors introduced here described the design and characterization of high-affinity heparin/HS-binding peptides that were modeled from the proposed consensus sequences of native heparin/HS-binding proteins [Verrecchio, A., Germann, M.W., Schick, B.P., Kung, B., Twardowsky, T., and San-Antonio, J.D. (2000) J. Biol. Chem., 275, 7701-7707]. They initially prepared peptide constructs, (AKKARA)n and (ARKKAAKA)n (n=1~6), Affinity coelectrophoresis revealed that low molecular weight (MW) peptides (n=1) had no affinity for heparin, but higher MW peptides exhibited significant affinity (Kd 50-150 nM), which increased with MW of the peptide. The affinity was strongest when sequence arrays were contiguous and alanines and arginines occupied hydrophobic and basic position, respectively. The higher MW peptides have also exhibited high affinities for total proteoglycan from endotヘ パ リ ン/ ヘ パ ラ ン硫 酸 (HS)は 、酵 素 、 増 殖 因子 、 サ イ ト

Peptides Containing Consensus Amino Acid Sequences for Binding to Heparin/Heparan Sulfate