Peptide Institute, Inc., 7-2-9 Saito-Asagi, Ibaraki-Shi, Osaka, 567-0085, Japan.
Chembiochem. 2019 Aug 16;20(16):2063-2069. doi: 10.1002/cbic.201900193. Epub 2019 Apr 18.
A novel solubilizing tag system for Asp/Asn/Glu/Gln-containing peptides is described. In this method, an Asp/Glu[Dbz-Cys-NH ]-containing peptide (Dbz: 3,4-diaminobenzoic acid) is first synthesized through fluorenylmethyloxycarbonyl (Fmoc) solid-phase peptide synthesis. The solubilizing moiety containing an oligo-Lys group is then attached to the peptide in hexafluoroisopropanol through a trityl anchor to afford a hydrophilic tagged peptide. To detach the solubilizing tag, the Dbz moiety of the tagged peptide is activated with NaNO , and the Asp/Asn/Glu/Gln-containing peptide is obtained through hydrolysis or ammonolysis. This synthetic approach proved to be compatible with native chemical ligation, and amyloid β-protein 1-42 was successfully synthesized by the solubilizing-tag-aided native chemical ligation-desulfurization method.
一种用于含有 Asp/Asn/Glu/Gln 的肽的新型增溶标签系统。在该方法中，首先通过芴甲氧羰基（Fmoc）固相肽合成合成含有 Asp/Glu[Dbz-Cys-NH ]的肽（Dbz：3,4-二氨基苯甲酸）。然后，通过三苯甲基锚将含有寡聚-Lys 基团的增溶部分连接到六氟异丙醇中的肽上，得到亲水性标记肽。为了去除增溶标签，用 NaNO 激活标记肽的 Dbz 部分，通过水解或氨解得到含有 Asp/Asn/Glu/Gln 的肽。该合成方法与天然化学连接兼容，通过增溶标签辅助的天然化学连接-脱硫方法成功合成了淀粉样β蛋白 1-42。
