In Vivo Imaging of Targeted Drug Delivery to Tumors Based on Fluorescence Resonance Energy Transfer and Optical Diffusion Tomography

2009 ◽  
Author(s):  
Vaibhav Gaind ◽  
Kevin J. Webb ◽  
Sumith A. Kularatne ◽  
Philip S. Low
Keyword(s):  
Drug Delivery ◽  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Targeted Drug Delivery ◽  
In Vivo Imaging ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Targeted Drug ◽  
Optical Diffusion Tomography

A target-initiated DNA network caged on magnetic particles for amplified chemiluminescence resonance energy transfer imaging of microRNA and targeted drug delivery

2016 ◽  
Vol 52 (87) ◽  
pp. 12841-12844 ◽  
Author(s):  
Sai Bi ◽  
Shuzhen Yue ◽  
Weiling Song ◽  
Shusheng Zhang
Keyword(s):  
Drug Delivery ◽  
Energy Transfer ◽  
Targeted Drug Delivery ◽  
Magnetic Particles ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Targeted Drug

DNA networks are constructed on magnetic particles by an initiator, which are functionalized for CRET imaging assay and targeted drug delivery.

Fluorescence resonance energy transfer monitoring of pH-responsive doxorubicin release from carbon dots/aptamer functionalized magnetic mesoporous silica

Nanomedicine ◽  
2021 ◽  
Author(s):  
Abolghasem Abbasi Kajani ◽  
Masoud Ayatollahi Mehrgardi
Keyword(s):  
Drug Delivery ◽  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Carbon Dots ◽  
Drug Loading ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Spectroscopic Techniques ◽  
Ph Responsive ◽  
Fluorescence Resonance

Aim: To develop a novel theranostic nanoplatform for simultaneous fluorescent monitoring and stimuli-triggered drug delivery. Materials & methods: Different microscopic and spectroscopic techniques were used for the characterization of nanocarriers. MCF-7 and human umbilical vein endothelial cell lines were cultured and treated with different doses of doxorubicin-loaded nanocarriers. The cell viability and drug release were studied using MTT assay and fluorescence microscopy. Results: Biocompatible and mono-disperse nanocarriers represent hollow and mesoporous structures with the calculated surface area of 552.83 m2.g-1, high magnetic activity (12.6 emu.g-1), appropriate colloidal stability and high drug loading capacity (up to 61%). Conclusion: Taxane-based carbon dots act as the pH-responsive gatekeepers for the controlled release of doxorubicin into cancer cells and provide a fluorescence resonance energy transfer system for real-time monitoring of drug delivery.

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 In Vivo Self-Interaction of Nodavirus RNA Replicase Protein A Revealed by Fluorescence Resonance Energy Transfer

2005 ◽  
Vol 79 (14) ◽  
pp. 8909-8919 ◽  
Author(s):  
Billy T. Dye ◽  
David J. Miller ◽  
Paul Ahlquist
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Mitochondrial Membrane ◽  
Rna Viruses ◽  
Protein A ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Rna Replication ◽  
Outer Mitochondrial Membrane

ABSTRACT Flock house virus (FHV) is the best-characterized member of the Nodaviridae, a family of small, positive-strand RNA viruses. Unlike most RNA viruses, FHV encodes only a single polypeptide, protein A, that is required for RNA replication. Protein A contains a C-proximal RNA-dependent RNA polymerase domain and localizes via an N-terminal transmembrane domain to the outer mitochondrial membrane, where FHV RNA replication takes place in association with invaginations referred to as spherules. We demonstrate here that protein A self-interacts in vivo by using flow cytometric analysis of fluorescence resonance energy transfer (FRET), spectrofluorometric analysis of bioluminescence resonance energy transfer, and coimmunoprecipitation. Several nonoverlapping protein A sequences were able to independently direct protein-protein interaction, including an N-terminal region previously shown to be sufficient for localization to the outer mitochondrial membrane (D. J. Miller and P. Ahlquist, J. Virol. 76:9856-9867, 2000). Mutations in protein A that diminished FRET also diminished FHV RNA replication, a finding consistent with an important role for protein A self-interaction in FHV RNA synthesis. Thus, the results imply that FHV protein A functions as a multimer rather than as a monomer at one or more steps in RNA replication.

scholarly journals Design of fluorescence resonance energy transfer (FRET)-based cGMP indicators: a systematic approach

2007 ◽  
Vol 407 (1) ◽  
pp. 69-77 ◽  
Author(s):  
Michael Russwurm ◽  
Florian Mullershausen ◽  
Andreas Friebe ◽  
Ronald Jäger ◽  
Corina Russwurm ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Systematic Approach ◽  
Dynamic Range ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Living Cells ◽  
Binding Domains ◽  
Fluorescence Resonance

The intracellular signalling molecule cGMP regulates a variety of physiological processes, and so the ability to monitor cGMP dynamics in living cells is highly desirable. Here, we report a systematic approach to create FRET (fluorescence resonance energy transfer)-based cGMP indicators from two known types of cGMP-binding domains which are found in cGMP-dependent protein kinase and phosphodiesterase 5, cNMP-BD [cyclic nucleotide monophosphate-binding domain and GAF [cGMP-specific and -stimulated phosphodiesterases, Anabaena adenylate cyclases and Escherichia coli FhlA] respectively. Interestingly, only cGMP-binding domains arranged in tandem configuration as in their parent proteins were cGMP-responsive. However, the GAF-derived sensors were unable to be used to study cGMP dynamics because of slow response kinetics to cGMP. Out of 24 cGMP-responsive constructs derived from cNMP-BDs, three were selected to cover a range of cGMP affinities with an EC50 between 500 nM and 6 μM. These indicators possess excellent specifity for cGMP, fast binding kinetics and twice the dynamic range of existing cGMP sensors. The in vivo performance of these new indicators is demonstrated in living cells and validated by comparison with cGMP dynamics as measured by radioimmunoassays.

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