Feldwisch Joachim, Tolmachev Vladimir
Affibody AB, Solna, Sweden.
Methods Mol Biol. 2012;899:103-26. doi: 10.1007/978-1-61779-921-1_7.
Affibody molecules are small and robust non-immunoglobulin affinity ligands capable of binding to a wide range of protein targets. They are selected from combinatorial libraries based on a 58 amino acid, three-alpha-helical Z-domain scaffold. They share no sequence or structural homologies to antibodies and in contrast to antibodies they can be functionally produced both by peptide synthesis and by recombinant expression in Escherichia coli. Protein engineering is used to adapt Affibody molecules binding to a target of interest to the specific demands imposed by the intended application. Obviously, the optimal molecule for molecular imaging will be different from the optimal molecule for therapy. Here, we describe general strategies to optimize Affibody molecules for diagnostic imaging and therapy applications.
亲和体分子是小型且稳定的非免疫球蛋白亲和配体，能够与多种蛋白质靶标结合。它们基于一个由58个氨基酸组成的三α螺旋Z结构域支架从组合文库中筛选得到。它们与抗体没有序列或结构同源性，与抗体不同的是，它们既可以通过肽合成也可以通过在大肠杆菌中重组表达来进行功能性生产。蛋白质工程用于使与感兴趣靶标结合的亲和体分子适应预期应用所提出的特定要求。显然，用于分子成像的最佳分子将不同于用于治疗的最佳分子。在此，我们描述了优化亲和体分子用于诊断成像和治疗应用的一般策略。
