The development of multichromophore assemblies has been of high interest to researchers in recent years, particularly in the development of light harvesting devices and organic electronics.  Interactions between conjugated systems generate unique photo-physical properties which differ from those found in the individual chromophores when precisely oriented in three-dimensional space.  Of the many strategies for building multichromophore arrays, utilization of self-assembling scaffolds found in nature have shown promise for facilitated self-assembly.  While the use of DNA to template self-assembly has been extensively studied in the past two decades, the use of self-assembling proteins, which offer advantages in stability and unique three-dimensional placement of chromophores, has been far less investigated.  Here, we examine the potential for using collagen, one of nature’s most abundant proteins, as a self-assembling scaffold for multichromophore assembly.  Chromophores are attached to the hydroxyl group of hydroxyproline modified collagen, and the effect on fluorescence is monitored as the collagen assembles into its characteristic triple-helix of three polyproline-II helices.  Simple modifications regarding linker length, chromophore spacing, and chromophore type are investigated to develop key insight in utilizing this novel scaffold for use in potential materials and sensing applications.<br/>

Investigation on the utilization of collagen as a scaffold for multichromophore assembly

251st National Meeting (2016)

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