Issue 24, 2016

Photophysics of GFP-related chromophores imposed by a scaffold design

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

Supplementary files

Article information

Article type
Paper
Submitted
30 Des 2015
Accepted
25 Feb 2016
First published
25 Feb 2016

Dalton Trans., 2016,45, 9884-9891

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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