Reagent has been reported in stapling of complex peptides as a photochemical trigger. Professor Amos Smith and coworkers have displayed this application in several recent reports.
The Journal of organic chemistry, 79(2), 759-768 (2013-12-24)
The design and synthesis of alanine-rich α-helical peptides constrained in a partially unfolded state by incorporation of the S,S-tetrazine phototrigger has been achieved, permitting, upon photochemical release, observation by 2D-IR spectroscopy of the subnanosecond conformational dynamics that govern the early
Journal of the American Chemical Society, 137(12), 4034-4037 (2015-03-21)
Protocols have been achieved that permit facile introduction of s-tetrazine into unprotected peptides and the protein, thioredoxin, between two cysteine sulfhydryl groups (i.e., staple), followed by photochemical release (i.e., unstaple) and regeneration of the peptide/protein upon removal of the cyano
The design, solid-phase synthesis, and photochemical validation of diverse peptide linchpins, containing the S,S-tetrazine phototrigger, have been achieved. Steady state irradiation or femtosecond laser pulses confirm their rapid photofragmentation. Attachment of peptides to the C- and N-termini will provide access
Proceedings of the National Academy of Sciences of the United States of America, 110(43), 17314-17319 (2013-10-10)
The relaxation of helical structures very close to equilibrium is observed via transient 2D IR spectroscopy. An initial distribution of synthetically distorted helices having an unnatural bridge linking the 10th and 12th residues of an alanine-rich α-helix is released to
Tetrazine phototriggers: probes for peptide dynamics.
Matthew J Tucker et al.
Angewandte Chemie (International ed. in English), 49(21), 3612-3616 (2010-04-15)
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