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Article

Steady-State and Time-Resolved Fluorescence Study of Selected Tryptophan-Containing Peptides in an AOT Reverse Micelle Environment

by
Krystian Gałęcki
1,*,
Agnieszka Kowalska-Baron
1,
Katarzyna E. Nowak
2,
Anna Gajda
3 and
Beata Kolesińska
3
1
Institute of Natural Products and Cosmetics, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, Stefanowskiego St. 2/22, 90-537 Lodz, Poland
2
Department of Oncobiology and Epigenetics, Faculty of Biology and Environmental Protection, University of Lodz, Pomorska St. 141/143, 90-236 Lodz, Poland
3
Institute of Organic Chemistry, Faculty of Chemistry, Lodz University of Technology, Żeromskiego St. 114, 90-924 Lodz, Poland
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2023, 24(20), 15438; https://doi.org/10.3390/ijms242015438
Submission received: 25 September 2023 / Revised: 20 October 2023 / Accepted: 20 October 2023 / Published: 22 October 2023
(This article belongs to the Special Issue Conformational Studies of Proteins and Peptides)
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Abstract

The aim of this study was to demonstrate the utility of time-resolved fluorescence spectroscopy in the detection of subtle changes in the local microenvironment of a tryptophan chromophore in a confined and crowded medium of AOT reverse micelles, which mimic biological membranes and cell compartmentalization. For this purpose, fluorescence properties of L-tryptophan and several newly synthesized tryptophan-containing peptides in buffer and in an AOT reverse micelle medium were determined. It was shown that insertion of tryptophan and its short di- and tripeptides inside micelles led to evident changes in both the steady-state emission spectra and in fluorescence decay kinetics. The observed differences in spectral characteristics, such as a blue shift in the emission maxima, changes in the average fluorescence lifetime, and the appearance of environmental-dependent fluorescent species, showed the utility of time-resolved fluorescence spectroscopy as a sensitive tool for detecting subtle conformational modifications in tryptophan and its peptides induced by changes in polarity, viscosity, and specific interactions between chromophores and water molecules/polar groups/ions that occur inside reverse micelles.
Keywords: tryptophan fluorescence; reverse micelles; fluorescence lifetime tryptophan fluorescence; reverse micelles; fluorescence lifetime

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MDPI and ACS Style

Gałęcki, K.; Kowalska-Baron, A.; Nowak, K.E.; Gajda, A.; Kolesińska, B. Steady-State and Time-Resolved Fluorescence Study of Selected Tryptophan-Containing Peptides in an AOT Reverse Micelle Environment. Int. J. Mol. Sci. 2023, 24, 15438. https://doi.org/10.3390/ijms242015438

AMA Style

Gałęcki K, Kowalska-Baron A, Nowak KE, Gajda A, Kolesińska B. Steady-State and Time-Resolved Fluorescence Study of Selected Tryptophan-Containing Peptides in an AOT Reverse Micelle Environment. International Journal of Molecular Sciences. 2023; 24(20):15438. https://doi.org/10.3390/ijms242015438

Chicago/Turabian Style

Gałęcki, Krystian, Agnieszka Kowalska-Baron, Katarzyna E. Nowak, Anna Gajda, and Beata Kolesińska. 2023. "Steady-State and Time-Resolved Fluorescence Study of Selected Tryptophan-Containing Peptides in an AOT Reverse Micelle Environment" International Journal of Molecular Sciences 24, no. 20: 15438. https://doi.org/10.3390/ijms242015438

APA Style

Gałęcki, K., Kowalska-Baron, A., Nowak, K. E., Gajda, A., & Kolesińska, B. (2023). Steady-State and Time-Resolved Fluorescence Study of Selected Tryptophan-Containing Peptides in an AOT Reverse Micelle Environment. International Journal of Molecular Sciences, 24(20), 15438. https://doi.org/10.3390/ijms242015438

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