Peptides constrained by ultrafast tetrazine phototriggers hold the potential to study the early kinetic events that take place during peptide/protein folding upon photochemical release by employing 2D-IR. A solid-phase synthetic route has been designed and validated to access a series of peptides containing the S,S-tetrazine phototrigger. The tetrazine tethered peptides can then be incorporated at various positions in larger peptide/protein systems via fragment coupling to explore peptide conformational dynamics.

Design, synthesis, and validation of tetrazine phototriggers to explore conformational dynamics of peptides

244th National Meeting (2012)

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