期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 140, 期 28, 页码 8671-8674出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.8b05425
关键词
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资金
- NSFC [21788102, 21722801, 21572058, 21402050, 21420102004]
- Programme of Introducing Talents of Discipline to Universities [B16017]
- Shanghai Rising-Star Program [16QA1401400]
Despite the rapid development of imaging techniques, precise probe localization and modulation in living cells is still a challenging task. Here we show that the simple hybridization between a photochromic fluorescent glycoprobe and human serum albumin (HSA) enables a unique fluorescence double-check mechanism for precisely localizing and manipulating probe molecules in living cells. Docking of a carbohydrate-modified naphthalimide (Naph)-spiropyran (SP) dyad to a hydrophobic pocket of HSA produces the glycoprobe-protein hybrid, causing the protein conformation to fold as determined by small-angle X-ray scattering. We show that the Naph and merocyanine (the photo isomer of SP) fluorescence of the resulting hybrid can be reversibly switched by light in buffer solution and in target cells overexpressing the carbohydrate receptor.
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