http://pubs.acs.org/doi/abs/10.1021/ol301490h
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 to diverse constrained peptide constructs that hold the promise of providing information about early peptide/protein conformational dynamics upon photochemical release.
The S,S-tetrazine scaffold possesses a number of advantages when compared to other nonreversible trigger systems: (1) flash photolysis can be conducted with near-UV (λ=355 or 410 nm) laser pulses, which would not lead to damage of the peptide; (2) acceptable photolysis yields are observed; and (3) the thiocyanate photoproducts are relatively inert and provide a potentially useful IR probe.
Our technical and applications support team can offer advice on library design and experimental set up and analysis. Relating to design, we can advise on the best overlap or offset of peptides to be used in your target application, Peptide Library Design
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