Work

Synthesis and Site-Specific Incorporation of Red-Shifted Azobenzene Amino Acids into Proteins

Year: 2015

Type: article

Abstract: A series of red-shifted azobenzene amino acids were synthesized in moderate-to-excellent yields via a two-step procedure in which tyrosine derivatives were first oxidized to the corresponding quinonoidal spirolactones followed by ceric ammonium nitrate-catalyzed azo formation with the substituted phenylhydrazines. The resulting azobenzene-alanine derivatives exhibited efficient trans/cis photoswitching upon irradiation with a blue (448 nm) or green (530 nm) LED light. Moreover, nine superfolder green fluorescent protein (sfGFP) mutants carrying the azobenzene-alanine analogues were expressed in E. coli in good yields via amber codon suppression with an orthogonal tRNA/PylRS pair, and one of the mutants showed durable photoswitching with the LED light.

Source: Organic Letters

DOI: 10.1021/acs.orglett.5b03268

Authors: Alford A. John, Carlo P. Ramil, Yulin Tian, Gang Cheng, Qing Lin

Institution: University at Buffalo, State University of New York

Language: English

Topic: Photochromic and Fluorescence Chemistry

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funders: State University of New York, National Institutes of Health, University at Buffalo, National Institute of General Medical Sciences