Fournier A, Saunders J K, St-Pierre S
Peptides. 1984 Mar-Apr;5(2):169-77. doi: 10.1016/0196-9781(84)90202-x.
VIP and related fragments were prepared by the solid-phase method. The peptides were assembled on a benzhydrylamine resin and couplings of the Boc-amino acids were carried out by the symmetrical anhydride method. Cleavage was achieved by treatment with liquid HF and purification was accomplished by successive steps of cation exchange, partition and semi-preparative high pressure liquid chromatography. The biological activities were evaluated in vitro in the rabbit perfused heart and in vivo on the rat blood pressure. Structural studies were performed by high resolution (400 MHz) 1H-NMR spectroscopy and circular dichroism. The results show that among all the fragments tested, only VIP2-28 retains significant biological activity. The fragments 1-14 and 15-28, which are devoid of activity, were found to be inactive as antagonists. VIP and some of the fragments tend to adopt the helical structure, as demonstrated by spectroscopic techniques.
血管活性肠肽（VIP）及相关片段采用固相法制备。肽段在二苯甲基胺树脂上组装，Boc - 氨基酸的偶联通过对称酸酐法进行。用液态氢氟酸处理实现裂解，通过阳离子交换、分配和半制备高压液相色谱的连续步骤完成纯化。在兔离体灌注心脏中进行体外生物活性评估，并在大鼠血压上进行体内评估。通过高分辨率（400 MHz）的1H - NMR光谱和圆二色性进行结构研究。结果表明，在所有测试片段中，只有VIP2 - 28保留显著的生物活性。发现无活性的片段1 - 14和15 - 28作为拮抗剂无活性。光谱技术表明，VIP和一些片段倾向于采用螺旋结构。
