Bcl-XL-binding helical peptides possessing d-Ala residues at their C-termini with the advantage of long-lasting intracellular stabilities.
Bcl-XL-binding helical peptides possessing d-Ala residues at their C-termini with the advantage of long-lasting intracellular stabilities.
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DOI：
10.1039/c7cc06904a
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发表时间：
2017-11
影响因子：
4.9
通讯作者：
Kagayaki Nogami;H. Tokumaru;Gouchi Isokawa;T. Oyoshi;K. Fujimoto;M. Inouye
中科院分区：
文献类型：
--
作者：
Kagayaki Nogami;H. Tokumaru;Gouchi Isokawa;T. Oyoshi;K. Fujimoto;M. Inouye
我们将d-Ala残基连接到基于促凋亡蛋白质Bad的交联螺旋肽的C-末端。d-Ala连接对Bcl-XL的二级结构和结合能力影响不大。结果表明，与原螺旋肽相比，d-Ala修饰的螺旋肽在细胞内的稳定性明显提高，并能有效地诱导细胞凋亡。
We attached d-Ala residues to cross-linked helical peptides based on the pro-apoptotic protein Bad at their C-termini. The d-Ala attachment had little influence on the secondary structures and binding abilities against Bcl-XL. The d-Ala attached helical peptides were much more stable in cells than original ones and efficiently induced apoptosis of the cells.