从头蛋白质模板半导体量子点的形成。

IF 10.4 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
ACS Central Science Pub Date : 2025-05-27 eCollection Date: 2025-06-25 DOI:10.1021/acscentsci.4c01826
Yueyu Yao, Jingyun Wu, Yue Hu, Laura Haubold, Obinna Uzosike, Guangming Cheng, Nan Yao, Gregory D Scholes, Michael H Hecht, Leah C Spangler
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引用次数: 0

摘要

在这里,我们提出了利用新生蛋白来调节硫化镉(cd)量子点大小的第一个实例。四种蛋白质被发现与CdS结合,并限制CdS量子点的生长,导致精确的尺寸控制,正如吸光度和荧光光谱所证明的那样。增加CdS的浓度不会改变吸光度和发射峰,从而表明蛋白质有效地限制了量子点的大小。使用不同的蛋白质也产生了具有不同光学和物理特性的量子点,包括当使用SynI3时生物介导纳米棒的外观。此外,新生蛋白有效地维持量子点的稳定性长达7天,超过了由小分子l-半胱氨酸覆盖的量子点的稳定性。封盖CdS的能力可能源于它们对Cd2+的亲和力,但对Cd2+的亲和力与所产生的量子点的大小之间似乎没有直接的相关性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
De Novo Proteins Template the Formation of Semiconductor Quantum Dots.

Here, we present the first instance of utilizing de novo proteins to regulate the size of cadmium sulfide (CdS) quantum dots. Four proteins were found to bind to CdS and cap the growth of CdS quantum dots, leading to precise size control, as evidenced by absorbance and fluorescence spectra. Increasing the concentration of CdS does not change the absorbance and emission peaks, thereby indicating that the proteins effectively constrain the size of the quantum dots. Employing different proteins also yielded quantum dots with distinct optical and physical properties, including the appearance of biomediated nanorods when SynI3 was utilized. Moreover, the de novo proteins effectively maintained the stability of the quantum dots for up to 7 days, surpassing the stability of quantum dots capped by the small molecule, l-cysteine. The ability to cap CdS likely stems from their affinities for Cd2+, yet there does not seem to be a direct correlation between the affinity for Cd2+ and the size of resulting quantum dots.

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来源期刊
ACS Central Science
ACS Central Science Chemical Engineering-General Chemical Engineering
CiteScore
25.50
自引率
0.50%
发文量
194
审稿时长
10 weeks
期刊介绍: ACS Central Science publishes significant primary reports on research in chemistry and allied fields where chemical approaches are pivotal. As the first fully open-access journal by the American Chemical Society, it covers compelling and important contributions to the broad chemistry and scientific community. "Central science," a term popularized nearly 40 years ago, emphasizes chemistry's central role in connecting physical and life sciences, and fundamental sciences with applied disciplines like medicine and engineering. The journal focuses on exceptional quality articles, addressing advances in fundamental chemistry and interdisciplinary research.
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