文献类型：期刊文献

英文题名：Photocontrolled Fluorescence "Double-Check" Bioimaging Enabled by a Glycoprobe-Protein Hybrid

作者：Fu, Youxin[1,2];Han, Hai-Hao[1,2];Zhang, Junji[1,2];He, Xiao-Peng[1,2];Feringa, Ben L.[1,2,3,4];Tian, He[1,2]

机构：[1]East China Univ Sci & Technol, Sch Chem & Mol Engn, Feringa Nobel Prize Scientist Joint Res Ctr, Key Lab Adv Mat, 130 Meilong Rd, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Sch Chem & Mol Engn, Feringa Nobel Prize Scientist Joint Res Ctr, Joint Int Res Lab Precis Chem & Mol Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China;[3]Univ Groningen, Fac Math & Nat Sci, Stratingh Inst Chem, Ctr Syst Chem, Nijenborgh 4, NL-9747 AG Groningen, Netherlands;[4]Univ Groningen, Fac Math & Nat Sci, Zernike Inst Adv Mat, Nijenborgh 4, NL-9747 AG Groningen, Netherlands

年份：2018

卷号：140

期号：28

起止页码：8671

外文期刊名：JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

收录：;EI(收录号：20182705399962);WOS:【SCI-EXPANDED(收录号:WOS:000439532000012)】；

基金：We thank the NSFC (Nos. 21788102, 21722801, 21572058, 21402050 and 21420102004), the Programme of Introducing Talents of Discipline to Universities (B16017) and the Shanghai Rising-Star Program (16QA1401400 to X.-P.H.) for generous financial support. We are also grateful to Dr. Na Li of the National Center for Protein Sciences Shanghai and the staff from BL19U2 beamline of the Shanghai Synchrotron Radiation Facility for data collection and processing of SAXS.

语种：英文

外文关键词：Bioimaging - Probes - Carbohydrates - Proteins - X ray scattering

摘要：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.