Heptapeptide mimic of ohmefentanyl binding in the discontinuous mu-opiod receptor.
Heptapeptide mimic of ohmefentanyl binding in the discontinuous mu-opiod receptor.
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不连续 mu-阿片受体中奥美芬太尼结合的七肽模拟物。
DOI：
10.1021/ol0509179
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发表时间：
2005
期刊：
影响因子：
5.2
通讯作者：
Greathouse,Denise
中科院分区：
文献类型：
--
作者：
Gawley,RobertE;Dukh,Mykhaylo;Cardona,ClaudiaM;Jannach,StephanH;Greathouse,Denise
羟甲芬太尼通过由170个残基分开的两个二肽序列（Trp-His和Asp-Tyr）与大鼠μ-阿片受体结合。一个转折诱导三肽，Pro-Aib-Aib，在THF中保持二肽的构象，结合麻醉剂（Kb= 7.1 × 104 M-1）。结合是特定的羟甲芬太尼超过吗啡，并伴随着构象变化的七肽主机。用Gly-Gly-Gly三肽连接二肽的对照实验显示没有结合的证据。
Ohmefentanyl binds to the rat μ-opiod receptor via two dipeptide sequences (Trp-His and Asp-Tyr) that are separated by 170 residues. A turn-inducing tripeptide, Pro-Aib-Aib, holds the dipeptides in a conformation that binds the narcotic (Kb= 7.1 × 104M-1) in THF. Binding is specific for ohmefentanyl over morphine and is accompanied by a conformational change in the heptapeptide host. Control experiments with a Gly-Gly-Gly tripeptide linking the dipeptides show no evidence of binding.