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The Role of Different Structural Motifs in the Ultrafast Dynamics of Second Generation Protein Stains

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Title The Role of Different Structural Motifs in the Ultrafast Dynamics of Second Generation Protein Stains
 
Creator CHATTERJEE, S
KARUSO, P
BOULANGE, A
PEIXOTO, PA
FRANCK, X
DATTA, A
 
Subject BASIS-SETS
EPICOCCONONE
FLUORESCENCE
CURCUMIN
PROTEOMICS
DIGESTION
 
Description Engineering the properties of fluorescent probes through modifications of the fluorophore structure has become a subject of interest in recent times. By doing this, the photophysical and photochemical properties of the modified fluorophore can be understood and this can guide the design and synthesis of better fluorophores for use in biotechnology. In this work, the electronic spectra and fluorescence decay kinetics of four analogues of the fluorescent natural product epicocconone were investigated. Epicocconone is unique in that the native state is weakly green fluorescent, whereas the enamine formed reversibly with proteins is highly emissive in the red. It was found that the ultrafast dynamics of the analogues depends profoundly on the H-bonding effect of solvents and solvent viscosity though solvent polarity also plays a role. Comparing the steady state and time-resolved data, the weak fluorescence of epicocconone in its native state is most likely due to the photoisomerization of the hydrocarbon side chain, while the keto enol moiety also has a role to play in determining the fluorescence quantum yield. This understanding is expected to aid the design of better protein stains from the same family.
 
Publisher AMER CHEMICAL SOC
 
Date 2014-10-16T15:31:15Z
2014-10-16T15:31:15Z
2013
 
Type Article
 
Identifier JOURNAL OF PHYSICAL CHEMISTRY B, 117(48)14951-14959
http://dx.doi.org/10.1021/jp4092927
http://dspace.library.iitb.ac.in/jspui/handle/100/15909
 
Language en