Ultrafast Polarized Fluorescence Measurements on Tryptophan and a Tryptophan-Containing Peptide

Larsen, Olaf F. A.; Stokkum, Ivo H. M. van; Pandit, Anjali; Grondelle, Rienk van; Amerongen, Herbert van

doi:10.1021/jp021756i

Cited by 26 publications

(24 citation statements)

References 29 publications

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“…This fast red decay component was recently also observed for free Trp and for single Trp in another small peptide, 25 but has not been observed before by others. For all samples, this fast red-shifted fluorescence decay component was somewhat slower than for free Trp (20-36 picoseconds compared to 13 picoseconds).…”

Section: Monomeric and Self-associated Melittin Contain Different Rotsupporting

confidence: 63%

“…As mentioned by Larsen et al, 25 the fast red decay component can also not be ascribed to fast internal L a -L b conversion. This effect takes place on a faster time scale (1.…”

Section: Different Fluorescence Lifetimes Reflect Differentmentioning

confidence: 74%

“…In Figure 2A, the DAS of Trp is also drawn for comparison (dotted spectra). The latter DAS is obtained from measurements of Larsen et al 25 Figure 3 shows the fluorescence center-of-gravity as a function of time, plotted for sample 1 and 2 in 3A and plotted for sample 3 in 3B. The DAS belonging to the ∼25 ps component has a very redshifted emission (centered around 420 nm), and therefore the centerof-gravity plots of all three samples show a fast blue shift, followed by a small red shift.…”

Section: Resultsmentioning

confidence: 98%

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Ultrafast Polarized Fluorescence Measurements on Monomeric and Self-Associated Melittin

et al. 2003

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The anisotropic and magic-angle fluorescence decay of the single tryptophan (Trp) residue of melittin, a bee venom peptide, was investigated by time-resolved fluorescence anisotropy using a streak camera setup. The peptide was dissolved either in distilled water or in Hepes/NaOH buffer containing low (10 mM) or high (2 M) concentrations of NaCl, the latter resulting in tetramerized melittin. For melittin in distilled water and low NaCl concentration, two anisotropy decay times were found in the order of ∼50 and ∼800 picoseconds, reflecting local and overall peptide dynamics, respectively, and for tetramerized melittin, two anisotropy decay times of ∼200 and ∼5500 picoseconds were found. Decay-associated spectra of the isotropic fluorescence decay show three time components in the range of ∼20 picoseconds, ∼500 picoseconds, and ∼3500 picoseconds, respectively. The relative amplitudes of the latter two change upon the self-association of melittin. This change can be explained by the existence of different rotamers of Trp in melittin, of which one is more favored in the melittin tetramer than in the melittin monomer.

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Section: Monomeric and Self-associated Melittin Contain Different Rotsupporting

confidence: 63%

“…As mentioned by Larsen et al, 25 the fast red decay component can also not be ascribed to fast internal L a -L b conversion. This effect takes place on a faster time scale (1.…”

Section: Different Fluorescence Lifetimes Reflect Differentmentioning

confidence: 74%

Section: Resultsmentioning

confidence: 98%

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Ultrafast Polarized Fluorescence Measurements on Monomeric and Self-Associated Melittin

et al. 2003

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“…Fluorescence decay measurements of the Trp zwitterion revealed two (or three, see ref. [67]) lifetimes, which were again attributed to 1 rotamers [28,68]. However, the assignment of the lifetimes to their respective conformations from NMR [69,70] has not been agreed upon [3].…”

Section: Nmrmentioning

confidence: 98%

“…Recently, supporting evidence for this view was provided by femtosecond resolution measurements. Short-lived decay components with lifetimes around 16 ps, attributable to rotamers, have been observed for Trp zwitterion [67] and for monellin [72]. On the other hand, the presence of a small amplitude, short lifetime component may be a predictor of excited-state conformer interconversion [73] or spectral relaxation [6].…”

Section: Nmrmentioning

confidence: 99%

How Do Rotameric Conformations Influence the Time-Resolved Fluorescence of Tryptophan in Proteins? A Perspective Based on Molecular Modeling and Quantum Chemistry

Moors¹,

Jonckheer²,

Maeyer³

et al. 2008

CPPS

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We discuss the dynamics of tryptophan rotamers in the context of the non-exponential fluorescence decay in proteins. The central question is: how does the ground-state conformational heterogeneity influence the time evolution of tryptophan fluorescence? This problem is examined here from the theoretical perspective. Three methods at different levels of theory, and with different scopes and computational requirements are reviewed. The Dead-end elimination method is limited to side-chain dynamics and provides an efficient way to detect the stable tryptophan rotamers in a protein. Its application to the study of heterogeneous emission characteristics is illustrated. Molecular dynamics is aimed at the full phase space of the macromolecule in solution, but must rely on classical force fields and laws of evolution. We examine to what extent the molecular mechanics paradigm yields sufficiently accurate thermodynamic results, and what are the possible kinetic implications. Finally Quantum Chemistry is the only theoretical method that allows a direct assessment of the excited states. It is necessarily restricted to small molecular systems, and thus must be used in a hybrid combination with classical methods and electrostatic models. So far understanding of the emitting state has greatly progressed as a result of these calculations, but the actual treatment of the photophysical decay processes at the quantum level has not yet really started.

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Self‐assembly of the octapeptide lanreotide and lanreotide‐based derivatives: the role of the aromatic residues

Pandit

Fay

Bordes

et al. 2007

Journal of Peptide Science

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We investigated the spectroscopic properties of the aromatic residues in a set of octapeptides with various self-assembly properties. These octapeptides are based on lanreotide, a cyclic peptide analogue of somatostatin-14 that spontaneously self-assembles into very long and monodisperse hollow nanotubes. A previous study on these lanreotide-based derivatives has shown that the disulfide bridge, the peptide hairpin conformation and the aromatic residues are involved in the self-assembly process and that modification of these properties either decreases the self-assembly propensity or modifies the molecular packing resulting in different self-assembled architectures. In this study we probed the local environment of the aromatic residues, naphthyl-alanine, tryptophan and tyrosine, by Raman and fluorescence spectroscopy, comparing nonassembled peptides at low concentrations with the self-assembled ones at high concentrations. As expected, the spectroscopic characteristics of the aromatic residues were found to be sensitive to the peptide-peptide interactions. Among the most remarkable features we could record a very unusual Raman spectrum for the tyrosine of lanreotide in relation to its propensity to form H-bonds within the assemblies. In Lanreotide nanotubes, and also in the supramolecular architectures formed by its derivatives, the tryptophan side chain is water-exposed. Finally, the low fluorescence polarization of the peptide aggregates suggests that fluorescence energy transfer occurs within the nanotubes.

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Ultrafast Polarized Fluorescence Measurements on Tryptophan and a Tryptophan-Containing Peptide

Cited by 26 publications

References 29 publications

Ultrafast Polarized Fluorescence Measurements on Monomeric and Self-Associated Melittin

Ultrafast Polarized Fluorescence Measurements on Monomeric and Self-Associated Melittin

How Do Rotameric Conformations Influence the Time-Resolved Fluorescence of Tryptophan in Proteins? A Perspective Based on Molecular Modeling and Quantum Chemistry

Self‐assembly of the octapeptide lanreotide and lanreotide‐based derivatives: the role of the aromatic residues

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