scholarly journals Characterization of Protein Aggregation via Intrinsic Fluorescence Lifetime

2009 ◽  
Vol 131 (46) ◽  
pp. 16608-16609 ◽  
Author(s):  
Kristian H. Schlick ◽  
Candace K. Lange ◽  
Gregory D. Gillispie ◽  
Mary J. Cloninger
Keyword(s):  
Protein Aggregation ◽  
Fluorescence Lifetime ◽  
Intrinsic Fluorescence

Fluorescence lifetime spectroscopy: a new technique for the characterization of polyplexes

2014 ◽  
Author(s):  
Cosimo D’Andrea ◽  
Daniele Pezzoli ◽  
Chiara Malloggi ◽  
Alessia Candeo ◽  
Alessandro Volonterio ◽  
...  
Keyword(s):  
Fluorescence Lifetime ◽  
New Technique ◽  
A New Technique

Characterization of protein aggregation: The case of a therapeutic immunoglobulin

2007 ◽  
Vol 1774 (1) ◽  
pp. 146-153 ◽  
Author(s):  
Barthélemy Demeule ◽  
M. Jayne Lawrence ◽  
Alex F. Drake ◽  
Robert Gurny ◽  
Tudor Arvinte
Keyword(s):  
Protein Aggregation

scholarly journals Fluorescence lifetime imaging for the characterization of the biochemical composition of atherosclerotic plaques

2011 ◽  
Vol 16 (9) ◽  
pp. 096018 ◽  
Author(s):  
Jennifer Phipps ◽  
Yinghua Sun ◽  
Ramez Saroufeem ◽  
Nisa Hatami ◽  
Michael C. Fishbein ◽  
...  
Keyword(s):  
Fluorescence Lifetime ◽  
Biochemical Composition ◽  
Atherosclerotic Plaques ◽  
Fluorescence Lifetime Imaging ◽  
Lifetime Imaging

Assembly and characterization of a fluorescence lifetime spectroscopy system for skin lesions diagnostic

2015 ◽  
Author(s):  
Marcelo Saito Nogueira ◽  
Ramon Gabriel Teixeira Rosa ◽  
Sebastião Pratavieira ◽  
Camila de Paula D´Almeida ◽  
Cristina Kurachi
Keyword(s):  
Fluorescence Lifetime ◽  
Skin Lesions ◽  
Spectroscopy System

Phase-Resolved Fluorescence Spectral and Lifetime Characterization of Commercial Humic Substances

1997 ◽  
Vol 51 (7) ◽  
pp. 921-929 ◽  
Author(s):  
Sherry L. Hemmingsen ◽  
Linda B. McGown
Keyword(s):  
Steady State ◽  
Humic Substances ◽  
Direct Measurement ◽  
Fluorescence Lifetime ◽  
Spectral Features ◽  
Good Precision ◽  
Convenient Means ◽  
Accurate Comparison ◽  
Excitation Emission Matrices

Phase-resolved excitation-emission matrices (PREEMs) are shown to provide a unique visual representation of the intrinsic fluorescence properties of humic acids under a variety of solution conditions. The calculation of spectral peak ratios in PREEMs as well as steady-state excitation-emission matrices provides a convenient means for quantitating differences between the spectra with good precision. Absorbance correction is shown to be essential for accurate comparison among spectral features. Increased detail is available from PREEMs at various modulation frequencies that reveal the distribution of fluorescence lifetime contributions across the spectral surface. Direct measurement of fluorescence lifetime recovered three ranges of lifetime components in the humic substances, <1 ns, 2–5 ns, and 8–14 ns, that are consistent with previously reported lifetimes. PREEMs, which provide a concise “survey” of how the lifetimes change across the spectrum, may aid in pinpointing spectral regions that provide the best lifetime discrimination among samples.

scholarly journals Ordered Nano-Laminated Films and Fluorescence Dynamic Characterization of Tb-Bisphthalocyanine

2011 ◽  
Vol 233-235 ◽  
pp. 2682-2686 ◽  
Author(s):  
Chun Zheng ◽  
Sheng Nan Sun ◽  
Li Min Ma ◽  
B Marí ◽  
Hai Ning Cui
Keyword(s):  
Fluorescence Lifetime ◽  
Arachidic Acid ◽  
Water Interface ◽  
Dynamic Characterization ◽  
Layer Spacing ◽  
Langmuir Blodgett ◽  
Air Water Interface ◽  
Periodic Layered Structure ◽  
Fluorescence Dynamic

Stable monolayers of Tb (III) -ocat-4-n-nonyloxyphthalocyanine (TbPc2) and TbPc2 blended with amphibious arachidic acid (AA) on air-water interface have been obtained and their solid multilayers have been successfully deposited by Langmuir-Blodgett (LB) technique. The characteristics of their structure and fluorescence are disclosed. The multilayer has a periodic layered structure with a layer spacing of 2.2 nm. Fluorescence lifetime results suggest that the excitons exist by photo-excitation in the film of TbPc2.

scholarly journals Development and Applications of a Broad-Coverage, TR-FRET-Based Kinase Binding Assay Platform

2009 ◽  
Vol 14 (8) ◽  
pp. 924-935 ◽  
Author(s):  
Connie S. Lebakken ◽  
Steven M. Riddle ◽  
Upinder Singh ◽  
W. Jack Frazee ◽  
Hildegard C. Eliason ◽  
...  
Keyword(s):  
Fluorescence Lifetime ◽  
Drug Targets ◽  
Kinase Inhibitors ◽  
Binding Assay ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Kinase Assay ◽  
Time Resolved ◽  
Traditional Activity

The expansion of kinase assay technologies over the past decade has mirrored the growing interest in kinases as drug targets. As a result, there is no shortage of convenient, fluorescence-based methods available to assay targets that span the kinome. The authors recently reported on the development of a non-activity-based assay to characterize kinase inhibitors that depended on displacement of an Alexa Fluor® 647 conjugate of staurosporine (a “tracer”) from a particular kinase. Kinase inhibitors were characterized by a change in fluorescence lifetime of the tracer when it was bound to a kinase relative to when it was displaced by an inhibitor. Here, the authors report on improvements to this strategy by reconfiguring the assay in a time-resolved fluorescence resonance energy transfer (TR-FRET) format that simplifies instrumentation requirements and allows for the use of a substantially lower concentration of kinase than was required in the fluorescence-lifetime-based format. The authors use this new assay to demonstrate several aspects of the binding assay format that are advantageous relative to traditional activity-based assays. The TR-FRET binding format facilitates the assay of compounds against low-activity kinases, allows for the characterization of type II kinase inhibitors either using nonactivated kinases or by monitoring compound potency over time, and ensures that the signal being detected is specific to the kinase of interest and not a contaminating kinase.

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