FRET study in oligopeptide-linked donor-acceptor system in PVA matrix

Sunil Shah, Wlodek Mandecki, Ji Li, Zygmunt Gryczynski, Julian Borejdo, Ignacy Gryczynski, Rafal Fudala

Research output: Contribution to journalArticleResearchpeer-review

Abstract

An oligopeptide: Lys-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys-NH2, cleaved specifically by a matrix metalloproteinase 9 (MMP-9) at the Ser-Leu bond, was labeled on the ε-NH2 groups of lysine with donor (5, 6 TAMRA) and acceptor (HiLyte647) dye. The donor control was a peptide labeled with 5, 6 TAMRA only on the C-terminal lysine, and the acceptor control was free HiLyte647. Following three products were studied by dissolving in 10% (w/w) poly(vinyl alcohol) and dried on glass slides forming 200 micron films. Absorption spectra of the films show full additivity of donor and acceptor absorptions. A strong Fluorescence Resonance Energy Transfer (FRET) with an efficiency of about 85% was observed in the fluorescence emission and excitation spectra. The lifetime of the donor was shorter and heterogeneous compared with the donor control.

Original languageEnglish
Number of pages1
JournalMethods and applications in fluorescence
Volume4
Issue number4
DOIs
StatePublished - 13 Dec 2016

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Oligopeptides
resonance fluorescence
lysine
energy transfer
Lysine
matrices
Matrix Metalloproteinase 9
chutes
Peptides
peptides
Absorption spectra
dissolving
emission spectra
alcohols
Alcohols
Coloring Agents
Dyes
dyes
Fluorescence
absorption spectra

Cite this

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title = "FRET study in oligopeptide-linked donor-acceptor system in PVA matrix",
abstract = "An oligopeptide: Lys-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys-NH2, cleaved specifically by a matrix metalloproteinase 9 (MMP-9) at the Ser-Leu bond, was labeled on the ε-NH2 groups of lysine with donor (5, 6 TAMRA) and acceptor (HiLyte647) dye. The donor control was a peptide labeled with 5, 6 TAMRA only on the C-terminal lysine, and the acceptor control was free HiLyte647. Following three products were studied by dissolving in 10{\%} (w/w) poly(vinyl alcohol) and dried on glass slides forming 200 micron films. Absorption spectra of the films show full additivity of donor and acceptor absorptions. A strong Fluorescence Resonance Energy Transfer (FRET) with an efficiency of about 85{\%} was observed in the fluorescence emission and excitation spectra. The lifetime of the donor was shorter and heterogeneous compared with the donor control.",
author = "Sunil Shah and Wlodek Mandecki and Ji Li and Zygmunt Gryczynski and Julian Borejdo and Ignacy Gryczynski and Rafal Fudala",
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language = "English",
volume = "4",
journal = "Methods and applications in fluorescence",
issn = "2050-6120",
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FRET study in oligopeptide-linked donor-acceptor system in PVA matrix. / Shah, Sunil; Mandecki, Wlodek; Li, Ji; Gryczynski, Zygmunt; Borejdo, Julian; Gryczynski, Ignacy; Fudala, Rafal.

In: Methods and applications in fluorescence, Vol. 4, No. 4, 13.12.2016.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - FRET study in oligopeptide-linked donor-acceptor system in PVA matrix

AU - Shah, Sunil

AU - Mandecki, Wlodek

AU - Li, Ji

AU - Gryczynski, Zygmunt

AU - Borejdo, Julian

AU - Gryczynski, Ignacy

AU - Fudala, Rafal

PY - 2016/12/13

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AB - An oligopeptide: Lys-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys-NH2, cleaved specifically by a matrix metalloproteinase 9 (MMP-9) at the Ser-Leu bond, was labeled on the ε-NH2 groups of lysine with donor (5, 6 TAMRA) and acceptor (HiLyte647) dye. The donor control was a peptide labeled with 5, 6 TAMRA only on the C-terminal lysine, and the acceptor control was free HiLyte647. Following three products were studied by dissolving in 10% (w/w) poly(vinyl alcohol) and dried on glass slides forming 200 micron films. Absorption spectra of the films show full additivity of donor and acceptor absorptions. A strong Fluorescence Resonance Energy Transfer (FRET) with an efficiency of about 85% was observed in the fluorescence emission and excitation spectra. The lifetime of the donor was shorter and heterogeneous compared with the donor control.

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