【摘要】 以β2 GP 为目标分子 ,在噬菌体表面展示肽库中进行亲和性筛选 ,经过 4轮筛选后 ,噬菌体的收率从 2 .4× 10 -5 %提高到 1.1× 10 -3 % .随机挑取噬菌体克隆 ,测定其与 β2 GP 的结合活性 ,选取其中结合力较强的克隆进行 DNA序列测定 ,得到一组保守序列( YFSAF) ,经与人凝血酶受体前体序列 ( 2 71～ 2 78)比较 ,发现它们具有明显的相似性 .经竞争性 ELISA分析实验 ,含有该序列的噬菌体克隆能够抑制β2 GP 与抗磷脂抗体的结合 ,抑制率可达 2 0 %左右更多还原

【Abstract】 Glycoprotein Ⅰ(β 2GPⅠ) has been identified as a cofactor in the recognition of the antiphospholipid antibodies(aPL). In order to select β 2GPⅠ recognizing molecules, β 2GPⅠ was used as a probe to screen affinity phage clones panning from a phage peptide library. After four rounds of selection, the phage recovery increased from 2.4×10 -5 % to 1.1×10 -3 %, indicating that the specific enrichment was achieved. In order to characterize these phage clones, we investigated their specific binding to β 2GPⅠ and their inhibition of β 2GPⅠ binding to anti β 2GPⅠ antibodies. Among them, the sequence motif (YFASF) was identified by DNA sequencing. The selected sequence and human thrombin receptor precursor (271~278) show similarities at several positions. The result proves the role of β 2GPⅠ in antiphospholipid syndrome.更多还原