Key Laboratory of Tropical Biological Resources, Ministry of Education, School of Life and Pharmaceutical Sciences, Hainan University, Haikou 570228, China.
Medical School, Guangxi University, Nanning 530004, China.
Bioorg Chem. 2021 Jul;112:104875. doi: 10.1016/j.bioorg.2021.104875. Epub 2021 Mar 29.
Head-to-tail cyclization is an effective strategy to improve the biological stability of peptides. The α-conotoxin [S9A]TxID is a peptide that inhibits α3β4 nAChR with high activity and selectivity. Herein, we established a method for cyclizing and oxidative folding of [S9A]TxID, and six cyclic analogues of [S9A]TxID were chemically synthesized with various linker lengths. We used the electrophysiology assay to measure activity values of these cyclic analogues, and obtained the most potent analogue c[S9A]TxID-6, which was more stable than native [S9A]TxID against proteinase K.
头对尾环化是提高肽类生物稳定性的有效策略。α-芋螺毒素 [S9A]TxID 是一种对 α3β4 nAChR 具有高活性和选择性的肽。本文建立了一种环化和氧化折叠 [S9A]TxID 的方法，并通过化学合成方法得到了具有不同连接长度的 [S9A]TxID 的六个环类似物。我们用电生理学检测方法测量了这些环类似物的活性值，得到了最有效的类似物 c[S9A]TxID-6，它比天然 [S9A]TxID 对蛋白酶 K 更稳定。
