School of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Tel Aviv, 69978, Israel.
Department of Chemistry, The University of Texas at Austin, 105 E 24th street A5300, Austin, TX, 78712-1224, USA.
Chem Commun (Camb). 2021 Oct 28;57(86):11386-11389. doi: 10.1039/d1cc05217a.
We report a chemiluminescent probe (CLPT1) that permits the paired detection of tyrosinase (Tyr) and biological thiols. Tyr only leads to a poor chemiluminescence response, a finding ascribed to the formation of a stable -benzoquinone intermediate. The addition of glutathione (GSH), or ascorbate to the -benzoquinone intermediate results in thiol conjugation or reduction to this intermediate, respectively. This produces a strong chemiluminescence response. Thiol co-dependence was demonstrated in live cells using the cell permeable analogue, CLPT3. The present chemiluminescence-based strategy allows the concurrent detection of tyrosinase activity and biological thiols.
我们报告了一种化学发光探针 (CLPT1)，它可以同时检测酪氨酸酶 (Tyr) 和生物硫醇。Tyr 仅导致较差的化学发光响应，这一发现归因于稳定的 -苯醌中间体的形成。谷胱甘肽 (GSH) 或抗坏血酸添加到 -苯醌中间体中，分别导致硫醇的共轭或还原至该中间体。这产生了强烈的化学发光响应。使用细胞可渗透的类似物 CLPT3 在活细胞中证明了硫醇的共依赖性。本化学发光策略允许同时检测酪氨酸酶活性和生物硫醇。
