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Optimized and far-red-emitting variants of fluorescent protein eqFP611.
Chem Biol. 2008 Mar; 15(3):224-33.CB

Abstract

Fluorescent proteins (FPs) emitting in the far-red region of the spectrum are highly advantageous for whole-body imaging applications because scattering and absorption of long-wavelength light is markedly reduced in tissue. We characterized variants of the red fluorescent protein eqFP611 with bright fluorescence emission shifted up to 639 nm. The additional red shift is caused by a trans-cis isomerization of the chromophore. The equilibrium between the trans and cis conformations is strongly influenced by amino acid residues 143 and 158. Pseudo monomeric tags were obtained by further genetic engineering. For the red chromophores of eqFP611 variants, molar extinction coefficients of up to approximately 150,000 were determined by an approach that is not affected by the presence of molecules with nonfunctional red chromophores. The bright fluorescence makes the red-shifted eqFP611 variants promising lead structures for the development of near-infrared fluorescent markers. The red fluorescent proteins performed well in cell biological applications, including two-photon imaging.

Authors+Show Affiliations

Institute of General Zoology and Endocrinology, University of Ulm, 89069 Ulm, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18355722

Citation

Kredel, Simone, et al. "Optimized and Far-red-emitting Variants of Fluorescent Protein EqFP611." Chemistry & Biology, vol. 15, no. 3, 2008, pp. 224-33.
Kredel S, Nienhaus K, Oswald F, et al. Optimized and far-red-emitting variants of fluorescent protein eqFP611. Chem Biol. 2008;15(3):224-33.
Kredel, S., Nienhaus, K., Oswald, F., Wolff, M., Ivanchenko, S., Cymer, F., Jeromin, A., Michel, F. J., Spindler, K. D., Heilker, R., Nienhaus, G. U., & Wiedenmann, J. (2008). Optimized and far-red-emitting variants of fluorescent protein eqFP611. Chemistry & Biology, 15(3), 224-33. https://doi.org/10.1016/j.chembiol.2008.02.008
Kredel S, et al. Optimized and Far-red-emitting Variants of Fluorescent Protein EqFP611. Chem Biol. 2008;15(3):224-33. PubMed PMID: 18355722.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Optimized and far-red-emitting variants of fluorescent protein eqFP611. AU - Kredel,Simone, AU - Nienhaus,Karin, AU - Oswald,Franz, AU - Wolff,Michael, AU - Ivanchenko,Sergey, AU - Cymer,Florian, AU - Jeromin,Andreas, AU - Michel,Francois J, AU - Spindler,Klaus-Dieter, AU - Heilker,Ralf, AU - Nienhaus,G Ulrich, AU - Wiedenmann,Jörg, PY - 2007/10/22/received PY - 2008/01/14/revised PY - 2008/02/04/accepted PY - 2008/3/22/pubmed PY - 2008/5/24/medline PY - 2008/3/22/entrez SP - 224 EP - 33 JF - Chemistry & biology JO - Chem. Biol. VL - 15 IS - 3 N2 - Fluorescent proteins (FPs) emitting in the far-red region of the spectrum are highly advantageous for whole-body imaging applications because scattering and absorption of long-wavelength light is markedly reduced in tissue. We characterized variants of the red fluorescent protein eqFP611 with bright fluorescence emission shifted up to 639 nm. The additional red shift is caused by a trans-cis isomerization of the chromophore. The equilibrium between the trans and cis conformations is strongly influenced by amino acid residues 143 and 158. Pseudo monomeric tags were obtained by further genetic engineering. For the red chromophores of eqFP611 variants, molar extinction coefficients of up to approximately 150,000 were determined by an approach that is not affected by the presence of molecules with nonfunctional red chromophores. The bright fluorescence makes the red-shifted eqFP611 variants promising lead structures for the development of near-infrared fluorescent markers. The red fluorescent proteins performed well in cell biological applications, including two-photon imaging. SN - 1074-5521 UR - https://www.unboundmedicine.com/medline/citation/18355722/Optimized_and_far_red_emitting_variants_of_fluorescent_protein_eqFP611_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1074-5521(08)00079-3 DB - PRIME DP - Unbound Medicine ER -