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Issue 24, 2016
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Photophysics of GFP-related chromophores imposed by a scaffold design

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Abstract

In this paper, a rigid scaffold imposes the photophysics of chromophores with a benzylidene imidazolidinone core by mimicking the β-barrel structure of the green fluorescent protein (GFP) and its analogs. The designed artificial frameworks maintain fluorescence responses and, therefore, conformational rigidity of typically non-emissive GFP-related chromophores. To replicate a small weight percent of the chromophore inside the natural GFP, two synthetic approaches were utilized: coordinative immobilization and non-coordinative inclusion. Despite low chromophore loading in the rigid matrix, both approaches resulted in formation of photoluminescent hybrid materials. Furthermore, the rigid scaffold dictates chromophore fluorescence by replicating its behavior in solution or the solid state. The presented results open an avenue for utilization of rigid scaffolds in the engineering of materials with tunable photoluminescence profiles for a variety of practical applications.

Graphical abstract: Photophysics of GFP-related chromophores imposed by a scaffold design

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Publication details

The article was received on 30 Dec 2015, accepted on 25 Feb 2016 and first published on 25 Feb 2016


Article type: Paper
DOI: 10.1039/C5DT05063D
Dalton Trans., 2016,45, 9884-9891

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    Photophysics of GFP-related chromophores imposed by a scaffold design

    E. A. Dolgopolova, T. M. Moore, W. B. Fellows, M. D. Smith and N. B. Shustova, Dalton Trans., 2016, 45, 9884
    DOI: 10.1039/C5DT05063D

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