A close look at fluorescence quenching of organic dyes by tryptophan

Doose S, Neuweiler H, Sauer M (2005)
CHEMPHYSCHEM 6(11): 2277-2285.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Understanding fluorescence quenching processes of organic dyes by biomolecular compounds is of fundamental importance for in-vitro and in-vivo fluorescence studies. It has been reported that the excited singlet state of some oxazine and rhodamine derivatives is efficiently and almost exclusively quenched by the amino acid tryptophan (Trp) and the DNA base guanine via photoinduced electron transfer (PET). We present a detailed analysis of the quenching interactions between the oxazine dye MR121 and Trp in aqueous buffer. Steady-state and time-resolved fluorescence spectroscopy, together with fluorescence correlation spectroscopy (FCS), reveal three contributing quenching mechanisms: 1) diffusion-limited dynamic quenching with a bimolecular quenching rate constant k(d) of 4.0 x 10(9) s(-1) M-1, 2) static quenching with a bimolecular association constant K-s of 61 M-1, and 3) a sphere-of-action contribution to static quenching described by an exponential factor with a quenching constant lambda of 22 M-1. The latter two are characterized as nonfluorescent complexes, formed with approximate to 30% efficiency upon encounter, that are stable for tens of nanoseconds. The measured binding energy of 2030 kJmol(-1) is consistent with previous estimates from molecular dynamics simulations that proposed stacked complexes due to hydrophobic forces. We further evaluate the influence of glycerol and denaturant (guanidine hydrochloride) on the formation and stability of quenched complexes. Comparative measurements performed with two other dyes, ATTO 655 and Rhodamine 6G show similar results and thus demonstrate the general applicability of utilizing PET between organic dyes and Trp for the study of conformational dynamics of biopolymers on sub-nanometer length and nanosecond time-scales.
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Zeitschriftentitel
CHEMPHYSCHEM
Band
6
Zeitschriftennummer
11
Seite
2277-2285
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Doose S, Neuweiler H, Sauer M. A close look at fluorescence quenching of organic dyes by tryptophan. CHEMPHYSCHEM. 2005;6(11):2277-2285.
Doose, S., Neuweiler, H., & Sauer, M. (2005). A close look at fluorescence quenching of organic dyes by tryptophan. CHEMPHYSCHEM, 6(11), 2277-2285. doi:10.1002/cphc.200500191
Doose, S., Neuweiler, H., and Sauer, M. (2005). A close look at fluorescence quenching of organic dyes by tryptophan. CHEMPHYSCHEM 6, 2277-2285.
Doose, S., Neuweiler, H., & Sauer, M., 2005. A close look at fluorescence quenching of organic dyes by tryptophan. CHEMPHYSCHEM, 6(11), p 2277-2285.
S. Doose, H. Neuweiler, and M. Sauer, “A close look at fluorescence quenching of organic dyes by tryptophan”, CHEMPHYSCHEM, vol. 6, 2005, pp. 2277-2285.
Doose, S., Neuweiler, H., Sauer, M.: A close look at fluorescence quenching of organic dyes by tryptophan. CHEMPHYSCHEM. 6, 2277-2285 (2005).
Doose, S, Neuweiler, H, and Sauer, Markus. “A close look at fluorescence quenching of organic dyes by tryptophan”. CHEMPHYSCHEM 6.11 (2005): 2277-2285.

55 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

The initial step of DNA hairpin folding: a kinetic analysis using fluorescence correlation spectroscopy.
Kim J, Doose S, Neuweiler H, Sauer M., Nucleic Acids Res 34(9), 2006
PMID: 16687657
A microscopic view of miniprotein folding: enhanced folding efficiency through formation of an intermediate.
Neuweiler H, Doose S, Sauer M., Proc Natl Acad Sci U S A 102(46), 2005
PMID: 16269542

51 References

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Über die von der molekularkinetischen Theorie der Wärme geforderte Bewegung von in ruhenden Flüssigkeiten suspendierten Teilchen
Einstein, Annalen der Physik 322(8), 1905

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