Dolgikh D A, Uversky V N, Gabrielian A E, Chemeris V V, Federov A N, Navolotskaya E V, Zav'yalov V P, Kirpichnikov M P
Institute of Molecular Biology. Russian Academy of Sciences, Moscow.
Protein Eng. 1996 Feb;9(2):195-201. doi: 10.1093/protein/9.2.195.
The de novo protein albebetin has been designed recently to form a predetermined tertiary fold that has not yet been observed in natural proteins. An eight amino acid fragment (131-138) of human interferon alpha(2) carrying the blast-transforming activity of the protein was attached to the N-terminus of albebetin next to its initiatory methionine residue. The gene of chimeric protein was expressed in a wheat germ cell-free translation system and synthesized protein was tested for its compactness and stability. Its ability for receptor binding was also studied. We have shown that albebetin with attached octapeptide is practically as compact as natural proteins of corresponding molecular weight and possesses high stability toward the urea-induced unfolding. It binds murine thymocyte receptor at a high affinity and activates the thymocyte blast transformation efficiently at a concentration of 10(-11) M.
新型蛋白质阿尔贝贝汀（albebetin）最近被设计出来，以形成一种在天然蛋白质中尚未观察到的预定三级折叠结构。携带该蛋白质的原代转化活性的人干扰素α(2)的一个八氨基酸片段（131-138）连接到阿尔贝贝汀起始甲硫氨酸残基旁边的N端。嵌合蛋白的基因在小麦胚无细胞翻译系统中表达，并对合成的蛋白进行了紧密性和稳定性测试。还研究了其与受体结合的能力。我们已经表明，带有连接八肽的阿尔贝贝汀实际上与相应分子量的天然蛋白质一样紧密，并且对尿素诱导的去折叠具有高稳定性。它以高亲和力结合小鼠胸腺细胞受体，并在10^(-11) M的浓度下有效地激活胸腺细胞原代转化。
