Free instals Blank And Secure 7.662/18/2024 These experiments highlight the utility of this new protecting group for SPPS and biological experiments. Finally, uncaging of these protected peptides by either UV or two-photon activation was used to initiate their subsequent enzymatic processing by the enzyme farnesyltransferase. This reagent was then used to assemble two biologically relevant peptides and characterize their photolysis kinetics in both UV- and two-photon-mediated reactions a two-photon action cross-section of 0.71 – 1.4 GM for the new protecting group was particularly notable. Here we describe the synthesis of a new NDBF-based protecting group bearing a methoxy substituent and use it to prepare a protected form of cysteine suitable for SPPS. In earlier work, we explored the use of the nitrodibenzofuran (NDBF) group for thiol protection and found it to exhibit a faster rate towards UV photolysis relative to simple nitroveratryl-based protecting groups and a useful two-photon cross-section. In solid phase peptide synthesis (SPPS), the most common photoremovable group used for thiol protection is the o-nitrobenzyl group and related analogues. Photoremovable caging groups are useful for biological applications since the deprotection process can be initiated by illumination with light without the necessity of adding additional reagents such as acids or bases that can perturb biological activity.
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