Design, Synthesis, and Enzymatic Evaluation of Novel ZnO Quantum Dot-Based Assay for Detection of Proteinase 3 Activity,Bioconjugate Chemistry

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Design, Synthesis, and Enzymatic Evaluation of Novel ZnO Quantum Dot-Based Assay for Detection of Proteinase 3 Activity
Bioconjugate Chemistry ( IF 4.0 ) Pub Date : 2018-04-11 00:00:00 , DOI: 10.1021/acs.bioconjchem.8b00100
Jadwiga Popow-Stellmaszyk , Beata Bajorowicz , Anna Malankowska , Magdalena Wysocka , Tomasz Klimczuk ₁ , Adriana Zaleska-Medynska , Adam Lesner

Affiliation

Herein, the synthesis and application of functionalized quantum dot-based protease probes is described. Such probes are composed of nontoxic ZnO nanocrystals decorated by amino groups followed by linker and labeled peptide attachment. Spherical NH₂-terminated ZnO quantum dots (QDs) with the average size ranging from 4 to 8 nm and strong emission centered at 530 nm were prepared using the sol–gel method. The fluorescence of ZnO QDs was quenched by the BHQ1 moiety present on the N-terminal amino group of the peptide. The enzymatic cleavage of the peptide mediated by the proteinase 3 (PR3) bond resulted in an increase in the QD probe fluorescence. This observation was verified using both model and biological systems; and the picomolar detection limit was found to be more than 30 times lower than that of the previously reported internally quenched peptide (a decrease in detection limit from 43 to 1.3 pmol was observed).

中文翻译：

新型基于ZnO量子点的蛋白酶3活性检测方法的设计，合成和酶学评估

在此，描述了功能化的基于量子点的蛋白酶探针的合成和应用。此类探针由无毒的ZnO纳米晶体组成，这些晶体由氨基修饰，然后是连接子和标记的肽附着物。球形NH ₂使用溶胶-凝胶法制备了平均大小为4至8 nm且中心在530 nm处的强发射的ZnO末端的ZnO量子点（QDs）。ZnO QD的荧光被肽N端氨基上的BHQ1部分猝灭。蛋白酶3（PR3）键介导的肽的酶促切割导致QD探针荧光增加。使用模型和生物学系统都验证了这一观察结果；并且皮摩尔的检测限比先前报道的内部淬灭的肽低30倍以上（观察到的检测限从43 pmol降低至1.3 pmol）。

更新日期：2018-04-11

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