Perin F, Presentini R, Antoni G
Sclavo Research Centre, Siena, Italy.
J Chromatogr. 1987 Jun 26;397:365-70. doi: 10.1016/s0021-9673(01)85020-2.
It was recently shown that fragment 163-171 of human interleukin 1 beta (hIL1 beta) possesses interesting biological properties, as it presents immunostimulatory activity both in vitro and in vivo, whilst being apparently devoid of the strong inflammatory properties that prevent the possible therapeutic use of the entire interleukin 1 molecule. Therefore, this peptide may represent the fragment of the protein responsible for its immunostimulatory activity, distinct from the part involved in the inflammatory activity of the entire molecule. Large amounts of highly purified peptide are needed for an adequate pharmacological characterization, in view of its possible therapeutic applications. A suitable method for the preparation of this peptide, was therefore studied paying particular attention to the purification step, which is essentially based on an efficient use of preparative high-performance liquid chromatography.
最近有研究表明，人白细胞介素1β（hIL1β）的163 - 171片段具有有趣的生物学特性，因为它在体外和体内均呈现免疫刺激活性，同时明显缺乏阻止整个白细胞介素1分子进行可能的治疗应用的强烈炎症特性。因此，该肽段可能代表了蛋白质中负责其免疫刺激活性的片段，与整个分子参与炎症活性的部分不同。鉴于其可能的治疗应用，需要大量高度纯化的肽段进行充分的药理学表征。因此，研究了一种制备该肽段的合适方法，特别关注纯化步骤，该步骤主要基于高效使用制备型高效液相色谱法。
