从蝉花虫草提取的N6-(2-羟乙基)腺苷的降压活性及其与人血清白蛋白的相互作用

从蝉花虫草中提取分离了N ⁶-(2-羟乙基)腺苷N ⁶-(2-hydroxyethyl) -adenosine,HEA],对其降压机制及其与人血清白蛋白的相互作用进行了研究,揭示了降压机制以及在体内的传输机制。研究结果表明使用水沉醇提法提取HEA,HEA的纯度达到95%以上。HEA低（2.5mg/kg）、中（5mg/kg）、高（7.5mg/kg）浓度组腹腔注射高血压大鼠体内,HEA具有显著降压效果,中浓度组表现出较稳定的降压作用,其机制可能是激活腺苷A1受体。在HEA 与人血清白蛋白结合过程中,范德华力、氢键和疏水作用力是结合过程中的主要作用力,HEA在位点I与人血清白蛋白进行结合,结合过程轻微地改变人血清白蛋白的结构和微环境。分子对接结果表明,Ser-192、Lys-195、Arg-257、Ser-287和Arg-291是HEA与人血清白蛋白结合过程中重要的氨基酸残基。

N~6-(2-hydroxyethyl) adenosine(HEA) isolated from Ophiocordyceps sobolifera: its antihypertensive effect and interaction with human serum albumin

Antihypertensive effect and intravascular transport mechanism of N ⁶-(2-hydroxyethyl) adenosine (HEA) isolated from Ophiocordyceps sobolifera, and interaction between HEA and human serum albumin (HSA) were studied. HEA with purity over 95% was obtained by using water-sinking extraction. Intraperitoneal injection of HEA at low (2.5mg/kg), medium (5mg/kg), and high (7.5mg/kg) concentration showed significant antihypertensive effect on the rats suffered from hypertension, and medium concentration particularly showed more effectiveness. The antihypertensive mechanism of HEA might be activation of adenosine A1 receptor. Van der Waals force, hydrogen bonding and hydrophobic force were the main forces in the binding of HEA to human serum albumin. HEA bound to human serum albumin at site I. The structure and microenvironment of the human serum albumin was slightly changed during the binding process. Molecular docking results indicated that Ser-192, Lys-195, Arg-257, Ser-287 and Arg-291 were important amino acid residues for the interaction between HEA and human serum albumin.