Static and time-resolved fluorescence investigations of tryptophan analogues - a solvent study

Lotte K, Plessow R, Brockhinke A (2004)
PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES 3(4): 348-359.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
DOI
Autor*in
Lotte, Kirsten; Plessow, Regina; Brockhinke, AndreasUniBi
Einrichtung
Fakultät für Chemie > Physikalische Chemie I
Abstract / Bemerkung
The fluorescence properties of tryptophan, polytryptophan and seven of its analogues (7-azatryptophan, 5-hydroxytryptophan, 5-methoxytryptophan, 5-fluorotryptophan, 5-methyltryptophan, 5-bromotryptophan, and 6-fluorotryptophan) are studied using two novel fluorescence spectroscopic techniques for a wide range of solvent polarities. Two-dimensional mapping of all emission and all fluorescence spectra using excitation-emission spectroscopy (EES) has been used to determine quantum yields, positions of emission maxima, full widths at half maximum (FWHMs) as well as Stokes' shifts. Additionally, fluorescence lifetimes obtained from time-resolved experiments using a picosecond laser system are presented and compared with the data acquired from the static setup. This systematic study of the fluorescence characteristics is a prerequisite to assess the potential of these analogues to act as structure-conserving substitutes for tryptophan in protein fluorescence experiments. The potential of these analogues, to act as probes for the local environment, and allow estimation of the polarity in the vicinity of the fluorophore and its exposure to the solvent, is discussed.
Erscheinungsjahr
2004
Zeitschriftentitel
PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES
Band
3
Ausgabe
4
Seite(n)
348-359
ISSN
1474-905X
eISSN
1474-9092
Page URI
https://pub.uni-bielefeld.de/record/1608298

Zitieren

Lotte K, Plessow R, Brockhinke A. Static and time-resolved fluorescence investigations of tryptophan analogues - a solvent study. PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES. 2004;3(4):348-359.
Lotte, K., Plessow, R., & Brockhinke, A. (2004). Static and time-resolved fluorescence investigations of tryptophan analogues - a solvent study. PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES, 3(4), 348-359. https://doi.org/10.1039/b312436c
Lotte, Kirsten, Plessow, Regina, and Brockhinke, Andreas. 2004. “Static and time-resolved fluorescence investigations of tryptophan analogues - a solvent study”. PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES 3 (4): 348-359.
Lotte, K., Plessow, R., and Brockhinke, A. (2004). Static and time-resolved fluorescence investigations of tryptophan analogues - a solvent study. PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES 3, 348-359.
Lotte, K., Plessow, R., & Brockhinke, A., 2004. Static and time-resolved fluorescence investigations of tryptophan analogues - a solvent study. PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES, 3(4), p 348-359.
K. Lotte, R. Plessow, and A. Brockhinke, “Static and time-resolved fluorescence investigations of tryptophan analogues - a solvent study”, PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES, vol. 3, 2004, pp. 348-359.
Lotte, K., Plessow, R., Brockhinke, A.: Static and time-resolved fluorescence investigations of tryptophan analogues - a solvent study. PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES. 3, 348-359 (2004).
Lotte, Kirsten, Plessow, Regina, and Brockhinke, Andreas. “Static and time-resolved fluorescence investigations of tryptophan analogues - a solvent study”. PHOTOCHEMICAL AND PHOTOBIOLOGICAL SCIENCES 3.4 (2004): 348-359.

19 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Blue fluorescent amino acid for biological spectroscopy and microscopy.
Hilaire MR, Ahmed IA, Lin CW, Jo H, DeGrado WF, Gai F., Proc Natl Acad Sci U S A 114(23), 2017
PMID: 28533371
Solvent Dependence of Cyanoindole Fluorescence Lifetime.
Hilaire MR, Mukherjee D, Troxler T, Gai F., Chem Phys Lett 685(), 2017
PMID: 29225366
Kinetic modeling of demasking and hydrolysis of peptide bonds during proteolysis of β-lactoglobulin by trypsin.
Vorob'ev MM, Rao NM, Kochetkov KA., Dokl Biochem Biophys 471(1), 2016
PMID: 28058685
Origin of tryptophan fluorescence lifetimes part 1. Fluorescence lifetimes origin of tryptophan free in solution.
Albani JR., J Fluoresc 24(1), 2014
PMID: 23912963
Bioassays in natural product research - strategies and methods in the search for anti-inflammatory and antimicrobial activity.
Strömstedt AA, Felth J, Bohlin L., Phytochem Anal 25(1), 2014
PMID: 24019222
A spectroscopic survey of substituted indoles reveals consequences of a stabilized 1Lb transition.
Meng X, Harricharran T, Juszczak LJ., Photochem Photobiol 89(1), 2013
PMID: 22882557
Solvent effects on the steady state photophysics of estrone and 17β-estradiol.
Chan KY, Gavaghan BM, Stoeckel AW, Irizarry K, Hare PM., Photochem Photobiol 88(2), 2012
PMID: 22191459
Antimicrobial activity of peptides derived from human ß-amyloid precursor protein.
Papareddy P, Mörgelin M, Walse B, Schmidtchen A, Malmsten M., J Pept Sci 18(3), 2012
PMID: 22249992
Minimalist probes for studying protein dynamics: thioamide quenching of selectively excitable fluorescent amino acids.
Goldberg JM, Speight LC, Fegley MW, Petersson EJ., J Am Chem Soc 134(14), 2012
PMID: 22471784
Fluorescent analogs of biomolecular building blocks: design, properties, and applications.
Sinkeldam RW, Greco NJ, Tor Y., Chem Rev 110(5), 2010
PMID: 20205430
Urea facilitates the translocation of single-stranded DNA and RNA through the alpha-hemolysin nanopore.
Japrung D, Henricus M, Li Q, Maglia G, Bayley H., Biophys J 98(9), 2010
PMID: 20441749
Boosting antimicrobial peptides by hydrophobic oligopeptide end tags.
Schmidtchen A, Pasupuleti M, Mörgelin M, Davoudi M, Alenfall J, Chalupka A, Malmsten M., J Biol Chem 284(26), 2009
PMID: 19398550
Oligotryptophan-tagged antimicrobial peptides and the role of the cationic sequence.
Strömstedt AA, Pasupuleti M, Schmidtchen A, Malmsten M., Biochim Biophys Acta 1788(9), 2009
PMID: 19505433
Enzymatic digestion and antioxidant activity of the native and molten globule states of camel α-lactalbumin: Possible significance for use in infant formula
Salami Maryam, Yousefi Reza, Ehsani MohammadReza, Razavi SeyedHadi, Chobert Jean-Marc, Haertlé Thomas, Saboury AliAkbar, Atri MalihehSadat, Niasari-Naslaji Amir, Ahmad Faizan, Moosavi-Movahedi AliAkbar., Int Dairy J 19(9), 2009
PMID: IND44217551
Real-time cellular uptake of serotonin using fluorescence lifetime imaging with two-photon excitation.
Botchway SW, Parker AW, Bisby RH, Crisostomo AG., Microsc Res Tech 71(4), 2008
PMID: 18080329
The five bromotryptophans.
Bittner S, Scherzer R, Harlev E., Amino Acids 33(1), 2007
PMID: 17031473
Single- and multi-photon excited fluorescence from serotonin complexed with beta-cyclodextrin.
Bisby RH, Botchway SW, Dad S, Parker AW., Photochem Photobiol Sci 5(1), 2006
PMID: 16395437
Identification and reactivity of the triplet excited state of 5-hydroxytryptophan.
Dad S, Bisby RH, Clark IP, Parker AW., J Photochem Photobiol B 78(3), 2005
PMID: 15708522
Platinum(II) 1,10-phenanthroline complexes of acetylides containing redox-active groups.
Siemeling U, Bausch K, Fink H, Bruhn C, Baldus M, Angerstein B, Plessow R, Brockhinke A., Dalton Trans (14), 2005
PMID: 15995744

64 References

Daten bereitgestellt von Europe PubMed Central.


Holzwarth, 1995

Lakowicz, 1999

Brockhinke, Appl. Phys. B: Lasers Opt. B71(), 2000

Brockhinke, Phys. Chem. Chem. Phys. 5(), 2003
Hydrophobic clustering in acid-denatured IL-2 and fluorescence of a Trp NH-pi H-bond.
Nanda V, Liang SM, Brand L., Biochem. Biophys. Res. Commun. 279(3), 2000
PMID: 11162427
Aromatic amino acids are critical for stability of the bicoid homeodomain.
Subramaniam V, Jovin TM, Rivera-Pomar RV., J. Biol. Chem. 276(24), 2001
PMID: 11294843

Il'ichev, J. Phys. Chem. B 106(), 2002
Characterization of the emulsification properties of 2S albumins from sunflower seed.
Burnett GR, Rigby NM, Mills EN, Belton PS, Fido RJ, Tatham AS, Shewry PR., J Colloid Interface Sci 247(1), 2002
PMID: 16290454
Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state.
Tew DJ, Bottomley SP., J. Mol. Biol. 313(5), 2001
PMID: 11700071
Structure and dynamics of the alpha-lactalbumin molten globule: fluorescence studies using proteins containing a single tryptophan residue.
Chakraborty S, Ittah V, Bai P, Luo L, Haas E, Peng Z., Biochemistry 40(24), 2001
PMID: 11401570
pH-jump-induced folding and unfolding studies of barstar: evidence for multiple folding and unfolding pathways.
Rami BR, Udgaonkar JB., Biochemistry 40(50), 2001
PMID: 11735409
Probing the role of the F-helix in serpin stability through a single tryptophan substitution.
Cabrita LD, Whisstock JC, Bottomley SP., Biochemistry 41(14), 2002
PMID: 11926819
The effect of amino acid analogues on alkaline phosphatase. Formation in Escherichia coli K-12. II. Replacement of tryptophan by azatryptophan and by tryptazan.
Schlesinger S., J. Biol. Chem. 243(14), 1968
PMID: 4873680

Chen, J. Phys. Chem. 97(), 1993

Chen, J. Phys. Chem. 98(), 1994

Smirnov, J. Phys. Chem. B 101(), 1997

Rich, Photochem. Photobiol. 58(), 1993

Rich, J. Am. Chem. Soc. 117(), 1995
Biosynthetic incorporation of 7-azatryptophan into the phage lambda lysozyme: estimation of tryptophan accessibility, effect on enzymatic activity and protein stability.
Soumillion P, Jespers L, Vervoort J, Fastrez J., Protein Eng. 8(5), 1995
PMID: 8532666
Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors.
Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR., J. Biol. Chem. 271(9), 1996
PMID: 8617752

Guharay, Spectrochim. Acta, Part A 54(), 1998
A continuous fluorescence assay for tryptophan hydroxylase.
Moran GR, Fitzpatrick PF., Anal. Biochem. 266(1), 1999
PMID: 9887224
Characterization of aminoacyl-adenylates in B. subtilis tryptophanyl-tRNA synthetase, by the fluorescence of tryptophan analogs 5-hydroxytryptophan and 7-azatryptophan.
Hogue CW, Szabo AG., Biophys. Chem. 48(2), 1993
PMID: 8298054

Steward, J. Am. Chem. Soc. 119(), 1997
Regulatory properties of recombinant tropomyosins containing 5-hydroxytryptophan: Ca2+-binding to troponin results in a conformational change in a region of tropomyosin outside the troponin binding site.
Farah CS, Reinach FC., Biochemistry 38(32), 1999
PMID: 10441151
Fluorescence properties of recombinant tropomyosin containing tryptophan, 5-hydroxytryptophan and 7-azatryptophan.
Das K, Ashby KD, Smirnov AV, Reinach FC, Petrich JW, Farah CS., Photochem. Photobiol. 70(5), 1999
PMID: 10568167
A concerted tryptophanyl-adenylate-dependent conformational change in Bacillus subtilis tryptophanyl-tRNA synthetase revealed by the fluorescence of Trp92.
Hogue CW, Doublie S, Xue H, Wong JT, Carter CW Jr, Szabo AG., J. Mol. Biol. 260(3), 1996
PMID: 8757806
Study of complexes of a tryptophan-free mutant of E. coli trp aporepressor with tryptophan analogues using optically detected magnetic resonance (ODMR).
Ozarowski A, Wu JQ, Maki AH., FEBS Lett. 422(1), 1998
PMID: 9475168
Incorporation of tryptophan analogues into staphylococcal nuclease: stability toward thermal and guanidine-HCl induced unfolding.
Wong CY, Eftink MR., Biochemistry 37(25), 1998
PMID: 9636036
Incorporation of tryptophan analogues into staphylococcal nuclease, its V66W mutant, and Delta 137-149 fragment: spectroscopic studies.
Wong CY, Eftink MR., Biochemistry 37(25), 1998
PMID: 9636035
Phosphorescence and optically detected magnetic resonance characterization of the environments of tryptophan analogues in staphylococcal nuclease, its V66W mutant, and Delta 137-149 fragment.
Ozarowski A, Wu JQ, Davis SK, Wong CY, Eftink MR, Maki AH., Biochemistry 37(25), 1998
PMID: 9636037

Negrerie, J. Phys. Chem. 95(), 1991

Chen, Chem. Phys. Lett. 222(), 1994

Reichardt, Chem. Rev 94(), 1994

Plessow, J. Phys. Chem. B 104(), 2000

Beechem, 1991
Decomposition of protein tryptophan fluorescence spectra into log-normal components. I. Decomposition algorithms.
Burstein EA, Abornev SM, Reshetnyak YK., Biophys. J. 81(3), 2001
PMID: 11509382

Burstein, Photochem. Photobiol. 64(), 1996
Fluorescence quenching and isotope effect of tryptophan.
Eisinger J, Navon G., J Chem Phys 50(5), 1969
PMID: 5777485

Demas, J. Phys. Chem. 75(), 1971

Hermans, J. Opt. Soc. Am. 41(), 1951

Gilmore, J. Chem. Phys. 23(), 1955

Gilmore, J. Chem. Phys. 20(), 1952

Lippert, Z. Elektrochem. 61(), 1957

Taft, J. Am. Chem. Soc. 98(), 1976

Kamlet, Chem. Phys. Lett. 77(), 1981
Influence of steric bulk and electrostatics on the hydroxylation regiospecificity of tryptophan hydroxylase: characterization of methyltryptophans and azatryptophans as substrates.
Moran GR, Phillips RS, Fitzpatrick PF., Biochemistry 38(49), 1999
PMID: 10587452

Eftink, J. Phys. Chem. 94(), 1990

Twine, 2003

Guzow, Helv. Chim. Acta 84(), 2001

Ross, 1997

Kelepouris, J. Phys. Chem. A 104(), 2000

Borin, Chem. Phys. 262(), 2000

Catalan, J. Mol. Struct. 142(), 1986

Sengupta, Spectrochim. Acta, Part A 56(), 2000

Catalan, Chem. Phys. Lett. 368(), 2003

Kamlet, J. Am. Chem. Soc. 98(), 1976

Serrano-Andres, Int. J. Quantum Chem. 84(), 2001

Chapman, J. Phys. Chem. 96(), 1992

Eftink, J. Phys. Chem. 99(), 1995

Maroncelli, J. Chem. Phys. 86(), 1987
Fluorescence and the location of tryptophan residues in protein molecules.
Burstein EA, Vedenkina NS, Ivkova MN., Photochem. Photobiol. 18(4), 1973
PMID: 4583619

Lippert, Z. Naturforsch. A 10(), 1955

Kumar, Indian J. Pure Appl. Phys. 23(), 1985
Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 15052363
PubMed | Europe PMC

Suchen in

Google Scholar