Single crystals of optoelectronic materials that respond to external stimuli, such as mechanical, light, or heat, are immensely attractive for next generation smart materials. Here we report single crystals of a green fluorescent protein (GFP) chromophore analogue with irreversible mechanical bending and associated unusual enhancement of the fluorescence, which is attributed to the strained molecular packing in the perturbed region. Soft crystalline materials with such fluorescence intensity modulations occurring in response to mechanical stimuli under ambient pressure conditions will have potential implications for the design of technologically relevant tunable fluorescent materials.
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http://dx.doi.org/10.1002/anie.202007760 | DOI Listing |
Anal Biochem
March 2025
Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570, Japan. Electronic address:
Although Green Fluorescent Protein (GFP) is useful and most widely used, steric hindrance due to its size and the time required for chromophore formation are complications. However, it is difficult to form chromophores with peptides to reduce the molecular weight. Therefore, we focused on peptides that can become fluorescent by binding to dyes.
View Article and Find Full Text PDFAnal Chem
November 2024
Key Laboratory of the Ministry of Education for Advanced Catalysis Materials, College of Chemistry and Materials Science, Zhejiang Normal University, Jinhua 321004, Zhejiang, P. R. China.
J Phys Chem Lett
November 2024
Department of Chemistry, Kyungpook National University, Daegu 41566, Republic of Korea.
The excited-state dynamics of the GFP chromophore, HBDI (anionic -hydroxybenzylidene-2,3-dimethylimidazolinone), were investigated through a combination of theoretical nonadiabatic molecular dynamics (NAMD) simulations and femtosecond transient absorption spectroscopy (fs-TA). The NAMD simulations revealed that the primary dynamics in excited states involve the formation of a P-twisted intermediate (S), which undergoes pendulum-like oscillations with respect to ϕ = 90°. This motion serves as a reservoir for the excited-state population and the primary source of fluorescence.
View Article and Find Full Text PDFJ Phys Chem B
October 2024
Department of Chemistry and Chemical Biology, Indian Institute of Technology (Indian School of Mines) Dhanbad, Dhanbad826004, Jharkhand, India.
Three novel core green fluorescent protein (GFP) chromophore analogues, based on a doubly locked conformation and variable electronic effects by replacing one hydrogen with bromine, iodine, and methyl, respectively, have been synthesized to modulate the push-pull effect. These chromophores exhibited intramolecular H-bonding, as evidenced by single-crystal X-ray and H NMR studies. The fluorescence quantum yields (ϕ) of all of the chromophores were found to be more than an order of magnitude higher (∼0.
View Article and Find Full Text PDFSmall
October 2024
Optogenetics & Synthetic Biology Interdisciplinary Research Center, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Mei Long Road, Shanghai, 200237, China.
Fluorescent RNAs (FRs), which are RNA aptamers that bind and activate their cognate small fluorogenic dyes, have provided a particularly useful approach for imaging RNAs in live cells. Although the color palette of FRs is greatly expanded, a bright and stable cyan FR with good biocompatibility and biorthogonality with currently available FRs remains desirable but is not yet developed. Herein, the development of Myosotis is described, an RNA aptamer that emits bright cyan fluorescence upon binding a novel GFP chromophore-like fluorophore called DBT.
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