AMCA to TAMRA long range resonance energy transfer on a flexible peptide

A. Synak, Rafal Fudala, Ignacy Gryczynski, L. Kułak, S. Shah, I. E. Serdiuk, B. Grobelna, P. Arłukowicz, A. Kubicki, P. Bojarski

Research output: Contribution to journalArticleResearchpeer-review

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Abstract

Förster resonance energy transfer between 7-amino-4-methyl-3-coumarinylacetic acid, (AMCA, donor) and 5-carboxytetramethylrhodamine, (TAMRA, acceptor) bound to Lys(AMCA)-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys(TAMRA)-NH2 peptide is demonstrated by various spectroscopic techniques in glycerol at room temperature. In particular, nonexponential character of fluorescence intensity decay evidences the distance distribution between the donor and acceptor sites resulting from the flexibility of the peptide. Numerical analysis of the fluorescence decay yields the distance distribution parameters. The results obtained are consistent with those obtained from steady-state fluorescence indicating that energy transfer is more efficient than suggested by the relation between the critical distance and donor-acceptor distance for elongated peptide conformation.

Original languageEnglish
Pages (from-to)60-64
Number of pages5
JournalDyes and Pigments
Volume158
DOIs
StatePublished - 1 Nov 2018

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Tranexamic Acid
Energy transfer
Peptides
Fluorescence
Glycerol
Conformations
Numerical analysis
Acids
Temperature

Cite this

Synak, A. ; Fudala, Rafal ; Gryczynski, Ignacy ; Kułak, L. ; Shah, S. ; Serdiuk, I. E. ; Grobelna, B. ; Arłukowicz, P. ; Kubicki, A. ; Bojarski, P. / AMCA to TAMRA long range resonance energy transfer on a flexible peptide. In: Dyes and Pigments. 2018 ; Vol. 158. pp. 60-64.
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title = "AMCA to TAMRA long range resonance energy transfer on a flexible peptide",
abstract = "F{\"o}rster resonance energy transfer between 7-amino-4-methyl-3-coumarinylacetic acid, (AMCA, donor) and 5-carboxytetramethylrhodamine, (TAMRA, acceptor) bound to Lys(AMCA)-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys(TAMRA)-NH2 peptide is demonstrated by various spectroscopic techniques in glycerol at room temperature. In particular, nonexponential character of fluorescence intensity decay evidences the distance distribution between the donor and acceptor sites resulting from the flexibility of the peptide. Numerical analysis of the fluorescence decay yields the distance distribution parameters. The results obtained are consistent with those obtained from steady-state fluorescence indicating that energy transfer is more efficient than suggested by the relation between the critical distance and donor-acceptor distance for elongated peptide conformation.",
author = "A. Synak and Rafal Fudala and Ignacy Gryczynski and L. Kułak and S. Shah and Serdiuk, {I. E.} and B. Grobelna and P. Arłukowicz and A. Kubicki and P. Bojarski",
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Synak, A, Fudala, R, Gryczynski, I, Kułak, L, Shah, S, Serdiuk, IE, Grobelna, B, Arłukowicz, P, Kubicki, A & Bojarski, P 2018, 'AMCA to TAMRA long range resonance energy transfer on a flexible peptide', Dyes and Pigments, vol. 158, pp. 60-64. https://doi.org/10.1016/j.dyepig.2018.05.019

AMCA to TAMRA long range resonance energy transfer on a flexible peptide. / Synak, A.; Fudala, Rafal; Gryczynski, Ignacy; Kułak, L.; Shah, S.; Serdiuk, I. E.; Grobelna, B.; Arłukowicz, P.; Kubicki, A.; Bojarski, P.

In: Dyes and Pigments, Vol. 158, 01.11.2018, p. 60-64.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - AMCA to TAMRA long range resonance energy transfer on a flexible peptide

AU - Synak, A.

AU - Fudala, Rafal

AU - Gryczynski, Ignacy

AU - Kułak, L.

AU - Shah, S.

AU - Serdiuk, I. E.

AU - Grobelna, B.

AU - Arłukowicz, P.

AU - Kubicki, A.

AU - Bojarski, P.

PY - 2018/11/1

Y1 - 2018/11/1

N2 - Förster resonance energy transfer between 7-amino-4-methyl-3-coumarinylacetic acid, (AMCA, donor) and 5-carboxytetramethylrhodamine, (TAMRA, acceptor) bound to Lys(AMCA)-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys(TAMRA)-NH2 peptide is demonstrated by various spectroscopic techniques in glycerol at room temperature. In particular, nonexponential character of fluorescence intensity decay evidences the distance distribution between the donor and acceptor sites resulting from the flexibility of the peptide. Numerical analysis of the fluorescence decay yields the distance distribution parameters. The results obtained are consistent with those obtained from steady-state fluorescence indicating that energy transfer is more efficient than suggested by the relation between the critical distance and donor-acceptor distance for elongated peptide conformation.

AB - Förster resonance energy transfer between 7-amino-4-methyl-3-coumarinylacetic acid, (AMCA, donor) and 5-carboxytetramethylrhodamine, (TAMRA, acceptor) bound to Lys(AMCA)-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys(TAMRA)-NH2 peptide is demonstrated by various spectroscopic techniques in glycerol at room temperature. In particular, nonexponential character of fluorescence intensity decay evidences the distance distribution between the donor and acceptor sites resulting from the flexibility of the peptide. Numerical analysis of the fluorescence decay yields the distance distribution parameters. The results obtained are consistent with those obtained from steady-state fluorescence indicating that energy transfer is more efficient than suggested by the relation between the critical distance and donor-acceptor distance for elongated peptide conformation.

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M3 - Article

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