Development of caged non-hydrolyzable phosphoamino acids and application to photo-control of binding affinity of phosphopeptide mimetic to phosphopeptide-recognizing protein |
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| Affiliation: | 2. Departamento de Química Orgánica, Facultad de Ciencias, Universidad Autónoma de Madrid/IMDEA Nanociencia (TT), Cantoblanco, 28049 Madrid, Spain;3. Biodevice Nanotechnology Group, Agrotechnology and Food Sciences, Wageningen University, Postbus 8038, 6700 EK Wageningen, The Netherlands;1. CNR-IPCF, Largo Bruno Pontecorvo 3, I-56127 Pisa, Italy;2. Dipartimento di Fisica, Università di Pisa, Largo Bruno Pontecorvo 3, I-56127 Pisa, Italy;3. Dipartimento di Fisica, Università degli Studi di Perugia, Via A Pascoli 1, 06123 Perugia, Italy |
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| Abstract: | The design and synthesis of caged non-hydrolyzable phospho-serine, -threonine, and -tyrosine derivatives that generate parent non-hydrolyzable phosphoamino acids, containing a difluoromethylene unit instead of the oxygen of a phosphoester, after UV-irradiation are described. The caged non-hydrolyzable amino acids were incorporated into peptides by standard Fmoc solid-phase peptide synthesis, and the obtained peptides were successfully converted to the parent non-hydrolyzable phosphopeptides by UV-irradiation. Application of the caged non-hydrolyzable phosphoserine-containing peptide to photo-control the binding affinity of the peptide to 14-3-3β protein is also reported. |
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| Keywords: | Caged peptide Non-hydrolyzable Phosphoamino acid Phosphopeptide UV-responsive |
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