Fluorescence Resonance Energy Transfer Based Highly Efficient Theranostic Nanoplatform for Two-Photon Bioimaging and Two-Photon Excited Photodynamic Therapy of Multiple Drug Resistance Bacteria

2018 ◽  
Vol 1 (2) ◽  
pp. 298-309 ◽  
Author(s):  
Aruna Vangara ◽  
Avijit Pramanik ◽  
Ye Gao ◽  
Kaelin Gates ◽  
Salma Begum ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Photodynamic Therapy ◽  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Multiple Drug Resistance ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Multiple Drug ◽  
Two Photon ◽  
Highly Efficient

Fluorescence resonance energy transfer-based drug delivery systems for enhanced photodynamic therapy

2020 ◽  
Vol 8 (17) ◽  
pp. 3772-3788 ◽  
Author(s):  
Yu Huang ◽  
Feng Qiu ◽  
Rongjun Chen ◽  
Deyue Yan ◽  
Xinyuan Zhu
Keyword(s):  
Drug Delivery ◽  
Photodynamic Therapy ◽  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Drug Delivery Systems ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Delivery Systems ◽  
Recent Advances ◽  
Fluorescence Resonance

In this Review, recent advances in fluorescence resonance energy transfer-based drug delivery systems for enhanced photodynamic therapy are described, and the current challenges and perspectives in this emerging field are also discussed.

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.

Sign in / Sign up

Export Citation Format

Share Document