Genomics Research Center, Academia Sinica, No. 128, Section 2, Academia Road, Taipei 115, Taiwan; Institute of Chemistry, College of Science, University of the Philippines, Diliman, Quezon City 1101, Philippines.
Department of Chemistry, National Dong Hwa University, No. 1, Section 2, Da Hsueh Road, Shoufeng, Hualien 974, Taiwan.
Curr Opin Struct Biol. 2018 Jun;50:126-133. doi: 10.1016/j.sbi.2018.03.003. Epub 2018 Mar 16.
Heparan sulfate interacts with a variety of proteins at the cell surface. These proteins are primarily attracted to the high negative charge distribution brought by sulfate, sulfamate, and carboxylate functionalities along the sugar chain. Apart from electrostatic interactions, hydrogen bonding and even hydrophobic interactions contribute to the complex formation. While additional sulfate/sulfamate groups are often tolerated as long as the main structural requirements are met, occasionally, certain extra sulfate groups may be detrimental to the binding affinity. Here, we show these binding characteristics using the binding of fibroblast growth factors and heparin-binding hemagglutinin to synthetic heparan sulfate oligosaccharides as examples. Insights into the binding characteristics of these proteins may benefit future therapeutic interventions.
硫酸乙酰肝素与细胞表面的多种蛋白质相互作用。这些蛋白质主要被糖链上的硫酸基、磺酸盐基和羧酸盐功能基带来的高负电荷分布所吸引。除了静电相互作用外，氢键甚至疏水相互作用也有助于形成复合物。虽然只要满足主要结构要求，通常可以容忍额外的硫酸基/磺酸盐基，但有时某些额外的硫酸基可能会对结合亲和力有害。在这里，我们以成纤维细胞生长因子和肝素结合血凝素与合成硫酸乙酰肝素寡糖的结合为例，展示了这些结合特性。了解这些蛋白质的结合特性可能有助于未来的治疗干预。
