Binding of the growth factor glycyl-L-histidyl-L-lysine by heparin.
Binding of the growth factor glycyl-L-histidyl-L-lysine by heparin.
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生长因子甘氨酰-L-组氨酰-L-赖氨酸与肝素的结合。
DOI：
10.1016/0014-5793(95)01286-5
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发表时间：
1995
期刊：
影响因子：
3.5
通讯作者：
Hari,S
中科院分区：
文献类型：
--
作者：
Rabenstein,DL;Robert,JM;Hari,S
有证据表明，生长因子glycylhistidyl-lysine （GHK）与肝素结合，并通过[1H]NMR谱表征了这种相互作用。1H化学位移表明GHK与羧酸型和羧酸型肝素相互作用。化学位移数据与三质子化（ImH+, GlyNH3+, LysNH3+）形式的GHK与羧酸形式的肝素的弱离域结合一致。随着pD的增加和羧酸基的滴定，化学位移数据表明GHK的铵基与肝素羧酸基形成氢键，而组氨酸咪唑环占据肝素的咪唑结合位点。位点特异性结合的证据包括肝素的化学位移滴定曲线位移到较低pD，咪唑环电流增加了对特定肝素质子的屏蔽，以及GHK的化学位移滴定曲线位移到较高pD。根据化学位移与pD滴定数据，确定了羧酸型肝素结合GHK的特定结合常数（ImH+, GlyNH3+）， LysNH3+), （ImH+, GlyNH2, LysNH3+）和（Im, GlyNH3+, LysNH3+）形式。
Evidence is presented that the growth factor glycylhistidyl-lysine (GHK) binds to heparin, and the interaction has been characterized by [1H]NMR spectroscopy.1H chemical shifts indicate that GHK interacts with both the carboxylic acid and the carboxylate forms of heparin. The chemical shift data are consistent with a weak delocalized binding of the triprotonated (ImH+, GlyNH3+, LysNH3+) form of GHK by the carboxylic acid form of heparin. As the pD is increased and the carboxylic acid groups are titrated, chemical shift data indicate that ammonium groups of GHK are hydrogen bonded to heparin carboxylate groups, while the histidyl imidazolium ring occupies the imidazolium-binding site of heparin. Evidence for site-specific binding includes displacement of chemical shift titration curves for heparin to lower pD, increased shielding of specific heparin protons by the imidazolium ring current and displacement of chemical shift titration curves for GHK to higher pD. Specific binding constants were determined for binding of the (ImH+, GlyNH3+), LysNH3+), (ImH+, GlyNH2, LysNH3+) and (Im, GlyNH3+, LysNH3+) forms of GHK by the carboxylate form of heparin from chemical shift vs. pD titration data.