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Hydrophilic azaspiroalkenes as robust bioorthogonal reporters.

ABSTRACT: Two hydrophilic spiroalkenes, azaspiro[2.3]hex-1-ene and azaspiro[2.4]hept-1-ene, were designed and synthesized. Compared to the previously reported spiro[2.3]hex-1-ene, the azaspiroalkenes exhibited greater water solubility and reactivity as dipolarophiles in the photoinduced tetrazole-alkene cycloaddition reaction. In addition, an azaspiro[2.3]hex-1-ene-containing amino acid, AsphK, was found to be charged by an engineered pyrrolysyl-tRNA synthetase into proteins via amber codon suppression in E. coli as well as in mammalian cells.

SUBMITTER: An P

PROVIDER: S-EPMC6299827 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Hydrophilic azaspiroalkenes as robust bioorthogonal reporters.

An Peng P Wu Hsuan-Yi HY Lewandowski Tracey M TM Lin Qing Q

Chemical communications (Cambridge, England) 20181201 99

Two hydrophilic spiroalkenes, azaspiro[2.3]hex-1-ene and azaspiro[2.4]hept-1-ene, were designed and synthesized. Compared to the previously reported spiro[2.3]hex-1-ene, the azaspiroalkenes exhibited greater water solubility and reactivity as dipolarophiles in the photoinduced tetrazole-alkene cycloaddition reaction. In addition, an azaspiro[2.3]hex-1-ene-containing amino acid, AsphK, was found to be charged by an engineered pyrrolysyl-tRNA synthetase into proteins via amber codon suppression in ...[more]

PMID: 30483687

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