2003
DOI: 10.1021/jo0344891
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Caged Phospho-Amino Acid Building Blocks for Solid-Phase Peptide Synthesis

Abstract: Three 1-(2-nitrophenyl)ethyl-caged phospho-amino acids have been synthesized for use in standard N(alpha)-fluorenylmethoxycarbonyl-based solid-phase peptide synthesis (SPPS). The most common naturally occurring phospho-amino acids, serine, threonine, and tyrosine, were prepared as protected caged building blocks by modification with a unique phosphitylating reagent. In previous work, caged phospho-peptides were made using an interassembly approach (Rothman, D. M.; Vazquez, M. E.; Vogel, E. M.; Imperiali, B. Or… Show more

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Cited by 38 publications
(36 citation statements)
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“…The peptides were released from the resin with a C-terminal carboxylic acid and side-chain protection intact, and were subsequently derivatized to afford the corresponding C-terminal thioesters (Futaki et al 1997;Mezo et al 2001). The cpTyr building block was synthesized as previously described (Rothman et al 2003) to install a pTyr masked by the 1-(2-nitrophenyl)-ethyl (NPE) caging group. An N-terminal hexahistidine tag was included in the synthetic peptides to provide a handle for visualization and purification of ligation products after NCL.…”
Section: Resultsmentioning
confidence: 99%
“…The peptides were released from the resin with a C-terminal carboxylic acid and side-chain protection intact, and were subsequently derivatized to afford the corresponding C-terminal thioesters (Futaki et al 1997;Mezo et al 2001). The cpTyr building block was synthesized as previously described (Rothman et al 2003) to install a pTyr masked by the 1-(2-nitrophenyl)-ethyl (NPE) caging group. An N-terminal hexahistidine tag was included in the synthetic peptides to provide a handle for visualization and purification of ligation products after NCL.…”
Section: Resultsmentioning
confidence: 99%
“…Selected peptides were caged at the key phosphotyrosine residue using recently developed methodology (25). 1-(2-Nitrophenyl)ethyl (NPE) was chosen as the caging group because it satisfies key requirements of biologically useful caging groups and those of Fmoc-based solid phase peptide synthesis (19,33).…”
Section: Discussionmentioning
confidence: 99%
“…1-(2-Nitrophenyl)ethyl (NPE) was chosen as the caging group because it satisfies key requirements of biologically useful caging groups and those of Fmoc-based solid phase peptide synthesis (19,33). The NPE can be photochemically released with reasonable quantum efficiency at wavelengths around 350 nm (33,43), and the photo-byproduct, nitrosoacetophenone, is less harmful to cells than the corresponding aldehyde released by photolysis of commonly implemented o-nitrobenzyl caging groups (25).…”
Section: Discussionmentioning
confidence: 99%
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