Excited-state lifetime distributions of tryptophan fluorescence in polar solutions. Evidence for solvent exciplex formation

Векшин, Н. Л.; Vincent, Michel; Gallay, Jacques

doi:10.1016/0009-2614(92)87027-m

Cited by 30 publications

(22 citation statements)

References 28 publications

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“…2(d) shows the variation in each of the fluorescence decay component with increasing quencher concentration. The nature of the multi-exponential fluorescence decay of HSA, even in absence of any quencher, is consistent with the literature reports [50][51][52] and is mainly related to either a rotamer [53,54] or an exciplex model [55]. It is to be noted here that the lifetime of the individual components increase slightly ($0.6 to 0.8 ns) in presence of both SDZ and CAF, which seems little unusual and inconsistent with the observation that the static fluorescence intensity of HSA quenches in presence of these drugs (Fig.…”

Section: Analysis Of Trp Fluorescence Lifetime With Addition Of Sdz Asupporting

confidence: 81%

Caffeine and sulfadiazine interact differently with human serum albumin: A combined fluorescence and molecular docking study

Islam

Sonu

Gashnga

et al. 2016

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Section: Analysis Of Trp Fluorescence Lifetime With Addition Of Sdz Asupporting

confidence: 81%

Caffeine and sulfadiazine interact differently with human serum albumin: A combined fluorescence and molecular docking study

Islam

Sonu

Gashnga

et al. 2016

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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“…When the ~L a state is excited at 300 nm, the fluorescence light is emitted in the range 330-360 nm. Hence, for these excitation and emission wavelengths one lifetime of the tryptophan fluorescence is expected and this is indeed found in some cases, the most notable one being N-acetyltryptophanamide (NATA) with a lifetime of about 3 ns (Szabo and Rayner 1980;Wijnaendts van Resandt et al 1980;Robbins et al 1980;Ross et al 1981;Chang et al 1983;Wagner et al 1987;Bismuto et al 1991;Vekshin et al 1992). However, the amino acid tryptophan already exhibits two lifetimes (at neutral pH).…”

Section: Introductionmentioning

confidence: 94%

A long lifetime component in the tryptophan fluorescence of some proteins

et al. 1995

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The tryptophan fluorescence of two membrane proteins (outer membrane protein A and lactose permease), a 21-residue hydrophobic peptide, three soluble proteins (rat serum albumin, ribonuclease T1, and azurin), and N-acetyltryptophanamide (NATA) was investigated by time-resolved measurements extended over 65 ns. A long lifetime component with a characteristic time of 25 ns and an amplitude below 1% was found for outer membrane protein A, lactose permease, the peptide in lipid membranes, and azurin in water, but not for rat serum albumin, ribonuclease T1, and NATA in water. When outer membrane protein A was dissolved and unfolded in guanidinum hydrochloride, the long lifetime component disappeared. Hence, a hydrophobic environment seems to be a necessary requirement for the long lifetime component to be present. However, NATA dissolved in butanol does not exhibit the long lifetime component, while the peptide dissolved in the same solvent under conditions which preserve its helical structure does show the long lifetime. Thus, a regular secondary structure for the polypeptide chain to which the tryptophan residue belongs seems to be a second necessary requirement for the long lifetime component to be present. The long lifetime component may therefore be seen in the context of protein substates.

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“…The difficulty in observing negative ␣ i values for NATA is supported by more recent TRES obtained using TD (69,70) and FD measurements (I. Gryczynski et al, unpublished). Wavelength-dependent FD intensity decays for NATA in propylene glycol at Ϫ12ЊC are shown in Fig.…”

Section: Spectral Relaxation Of Trp/nata In Polar Solventsmentioning

confidence: 85%

On Spectral Relaxation in Proteins†¶‖

Lakowicz

2007

Photochemistry and Photobiology

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During the past several years there has been debate about the origins of nonexponential intensity decays of intrinsic tryptophan (trp) fluorescence of proteins, especially for single tryptophan proteins (STP). In this review we summarize the data from diverse sources suggesting that time‐dependent spectral relaxation is a ubiquitous feature of protein fluorescence. For most proteins, the observations from numerous laboratories have shown that for trp residues in proteins (1) the mean decay times increase with increasing observation wavelength; (2) decay associated spectra generally show longer decay times for the longer wavelength components; and (3) collisional quenching of proteins usually results in emission spectral shifts to shorter wavelengths. Additional evidence for spectral relaxation comes from the time‐resolved emission spectra that usually shows time‐dependent shifts to longer wavelengths. These overall observations are consistent with spectral relaxation in proteins occurring on a subnanosecond timescale. These results suggest that spectral relaxation is a significant if not dominant source of nonexponential decay in STP, and should be considered in any interpretation of nonexponential decay of intrinsic protein fluorescence.

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Excited-state lifetime distributions of tryptophan fluorescence in polar solutions. Evidence for solvent exciplex formation

Cited by 30 publications

References 28 publications

Caffeine and sulfadiazine interact differently with human serum albumin: A combined fluorescence and molecular docking study

Caffeine and sulfadiazine interact differently with human serum albumin: A combined fluorescence and molecular docking study

A long lifetime component in the tryptophan fluorescence of some proteins

On Spectral Relaxation in Proteins†¶‖

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