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Publication Abstract from PubMed

Human cellular retinol binding protein II (hCRBPII) was used as a protein engineering platform to rationally regulate absorptive and emissive properties of a covalently bound fluorogenic dye. We demonstrate the binding of a thio-dapoxyl analog via formation of a protonated imine between an active site lysine residue and the chromophore's aldehyde. Rational manipulation of the electrostatics of the binding pocket results in a 204 nm shift in absorption and a 131 nm shift in emission. The protein is readily expressed in mammalian systems and binds with exogenously delivered fluorophore as demonstrated by live-cell imaging experiments.

Regulation of Absorption and Emission in a Protein/Fluorophore Complex.,Santos EM, Chandra I, Assar Z, Sheng W, Ghanbarpour A, Bingham C, Vasileiou C, Geiger JH, Borhan B ACS Chem Biol. 2024 Jul 24. doi: 10.1021/acschembio.4c00125. PMID:39046136^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.