Tobacco Mosaic Virus (TMV) double-disks are a promising platform for exploring biomimetic light-harvesting. These complexes are stable at room temperature and can be modified with several different chromophores to evaluate the photodynamics of energy transfer. The full 34-mer protein complex is highly amenable to bioconjugations via both interior and exterior cysteines, and further bioconjugation handles can be added via the incorporation of non-canonical amino acids (ncAA) such as 3-nitrotyrosine. The incorporation of this ncAA, however, is not uniform across the peptide sequence, and TMV displays variable tolerance for 3-nitrotyrosine at different positions. Using computational modeling, we tested parameters such as hydrophobicity, solvation, and conformational flexibility to predict ncAA incorporation across TMV. We validated these predictions by expressing TMV variants incorporating 3-nitrotyrosine, and then gauged the assembly state using analytical HPLC. Furthermore, we developed a proxy assay using aminofluorescein to determine the likelihood that this side chain will couple with an aniline partner to eventually form a more complete biomimetic system.

Predictive design of tobacco mosaic virus double-disks for biomimetic light harvesting

ACS Spring Meeting 2021

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