A NIR-triggered gatekeeper of supramolecular conjugated unimicelles with two-photon absorption for controlled drug release

2019 ◽  
Vol 55 (47) ◽  
pp. 6735-6738 ◽  
Author(s):  
Yu Huang ◽  
Lingyue Shen ◽  
Dongbo Guo ◽  
Wumaier Yasen ◽  
Yan Wu ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Drug Release ◽  
Fluorescence Resonance Energy Transfer ◽  
Near Infrared ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Controlled Drug Release ◽  
Photon Absorption ◽  
Two Photon Absorption ◽  
Two Photon

Near-infrared-sensitive supramolecular hyperbranched conjugated unimicelles were constructed for controlled drug release via two-photon excited fluorescence resonance energy transfer.

scholarly journals Spatial Distribution and Function of Sterol Regulatory Element-Binding Protein 1a and 2 Homo- and Heterodimers by In Vivo Two-Photon Imaging and Spectroscopy Fluorescence Resonance Energy Transfer

2005 ◽  
Vol 25 (8) ◽  
pp. 2946-2956 ◽  
Author(s):  
Aikaterini Zoumi ◽  
Shrimati Datta ◽  
Lih-Huei L. Liaw ◽  
Cristen J. Wu ◽  
Gopi Manthripragada ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Regulatory Element ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Two Photon ◽  
Sterol Regulatory Element ◽  
Photon Imaging ◽  
Imaging And Spectroscopy

ABSTRACT Sterol regulatory element-binding proteins (SREBPs) are a subfamily of basic helix-loop-helix-leucine zipper proteins that regulate lipid metabolism. We show novel evidence of the in vivo occurrence and subnuclear spatial localization of both exogenously expressed SREBP-1a and -2 homodimers and heterodimers obtained by two-photon imaging and spectroscopy fluorescence resonance energy transfer. SREBP-1a homodimers localize diffusely in the nucleus, whereas SREBP-2 homodimers and the SREBP-1a/SREBP-2 heterodimer localize predominantly to nuclear speckles or foci, with some cells showing a diffuse pattern. We also used tethered SREBP dimers to demonstrate that both homo- and heterodimeric SREBPs activate transcription in vivo. Ultrastructural analysis revealed that the punctate foci containing SREBP-2 are electron-dense nuclear bodies, similar or identical to structures containing the promyelocyte (PML) protein. Immunofluorescence studies suggest that a dynamic interplay exists between PML, as well as another component of the PML-containing nuclear body, SUMO-1, and SREBP-2 within these nuclear structures. These findings provide new insight into the overall process of transcriptional activation mediated by the SREBP family.

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