Binding and cytotoxicity of I-131-labeled gastrin-releasing peptide receptor antagonists modified by cell penetrating peptides
Binding and cytotoxicity of I-131-labeled gastrin-releasing peptide receptor antagonists modified by cell penetrating peptides
复制标题
细胞穿透肽修饰的 131I 标记胃泌素释放肽受体拮抗剂的结合和细胞毒性
DOI：
10.1007/s10967-018-6307-1
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发表时间：
2019
影响因子：
1.6
通讯作者：
Wei Hongyuan
中科院分区：
文献类型：
--
作者：
Lv Minli;Zhao Peng;Zhuo Liangang;Liao Wei;Wang Hailin;Yang Xia;Wang Jing;Wang Guanquan;Song Hu;Feng Yue;Chen Yue;Yang Yuchuan;Wei Hongyuan
胃泌素释放肽受体(GRPR)是多种肿瘤中最有趣的过度表达靶点之一。由于GRPR拮抗剂类似物的优越潜力，它们在肿瘤放射成像和治疗领域得到了研究。然而，典型的拮抗剂存在无内化和结合亲和力差的缺点，阻碍了其在放射治疗中的应用。因此，我们尝试在RM26中引入低聚精氨酸(细胞穿透肽)，目的是增加与细胞的结合亲和力，甚至触发细胞内化。结果表明，Arg6作为最强的CPP，显著提高了RM26与GRPR的结合亲和力。
Gastrin releasing peptide receptors (GRPRs) are one of the most interesting targets over expressed in various tumors. Due to the superior potential of the GRPR antagonist analogs, they have been studied in the tumor radio imaging and therapy field. However, typical antagonists suffered the shortcomings of no internalization and poor binding affinity which hampered their applications in radiotherapy. Therefore, we attempted to introduce Oligoarginines (cell penetrating peptides) to RM26, aiming to increase the binding affinity or even trigger the internalization of the peptides on cells. The results showed Arg6as the most potent CPP, significantly enhanced the binding avidity of RM26 to the GRPR.