skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Resonance Energy Transfer in a Genetically Engineered Polypeptide Results in Unanticipated Fluorescence Intensity

Abstract

The fluorescence intensity of a C-terminal acceptor chromophore, N-(7-dimethylamino-4-methyl coumarin (DACM), increased proportionally with 280 nm irradiation of an increasing number of donor tryptophan residues located on a β-sheet forming polypeptide. The fluorescence intensity of the acceptor chromophore increased even as the length of the β-sheet edge approached 256 Å, well beyond the Förster radius for the tryptophan–acceptor chromophore pair. Here the folding of the peptides under investigation was verified by circular dichroism (CD) and deep UV resonance Raman experiments. Control experiments showed that the enhancement of DACM fluorescence occurred concomitantly with peptide folding. In other control experiments, the DACM fluorescence intensity of the solutions of tryptophan and DACM did not show any enhancement of DACM fluorescence with increasing tryptophan concentrations. Formation of fibrillar aggregates of the substrate peptides prepared for the fluorescence studies was undetectable by thioflavin T (ThT) fluorescence.

Authors:
 [1]; ORCiD logo [2];  [1];  [1]; ORCiD logo [1]
  1. Univ. at Albany, SUNY, Albany, NY (United States)
  2. Brookhaven National Lab. (BNL), Upton, NY (United States)
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1504878
Report Number(s):
BNL-211501-2019-JAAM
Journal ID: ISSN 0947-6539
Grant/Contract Number:  
SC0012704
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Chemistry - A European Journal
Additional Journal Information:
Journal Volume: 25; Journal Issue: 4; Journal ID: ISSN 0947-6539
Publisher:
ChemPubSoc Europe
Country of Publication:
United States
Language:
English
Subject:
77 NANOSCIENCE AND NANOTECHNOLOGY; energy transfer; fluorescence; peptides; photophysics; protein folding

Citation Formats

Seeley, Jason P., Cotlet, Mircea, Eagleton, Aileen M., Higashiya, Seiichiro, and Welch, John T. Resonance Energy Transfer in a Genetically Engineered Polypeptide Results in Unanticipated Fluorescence Intensity. United States: N. p., 2018. Web. doi:10.1002/chem.201804470.
Seeley, Jason P., Cotlet, Mircea, Eagleton, Aileen M., Higashiya, Seiichiro, & Welch, John T. Resonance Energy Transfer in a Genetically Engineered Polypeptide Results in Unanticipated Fluorescence Intensity. United States. doi:10.1002/chem.201804470.
Seeley, Jason P., Cotlet, Mircea, Eagleton, Aileen M., Higashiya, Seiichiro, and Welch, John T. Fri . "Resonance Energy Transfer in a Genetically Engineered Polypeptide Results in Unanticipated Fluorescence Intensity". United States. doi:10.1002/chem.201804470.
@article{osti_1504878,
title = {Resonance Energy Transfer in a Genetically Engineered Polypeptide Results in Unanticipated Fluorescence Intensity},
author = {Seeley, Jason P. and Cotlet, Mircea and Eagleton, Aileen M. and Higashiya, Seiichiro and Welch, John T.},
abstractNote = {The fluorescence intensity of a C-terminal acceptor chromophore, N-(7-dimethylamino-4-methyl coumarin (DACM), increased proportionally with 280 nm irradiation of an increasing number of donor tryptophan residues located on a β-sheet forming polypeptide. The fluorescence intensity of the acceptor chromophore increased even as the length of the β-sheet edge approached 256 Å, well beyond the Förster radius for the tryptophan–acceptor chromophore pair. Here the folding of the peptides under investigation was verified by circular dichroism (CD) and deep UV resonance Raman experiments. Control experiments showed that the enhancement of DACM fluorescence occurred concomitantly with peptide folding. In other control experiments, the DACM fluorescence intensity of the solutions of tryptophan and DACM did not show any enhancement of DACM fluorescence with increasing tryptophan concentrations. Formation of fibrillar aggregates of the substrate peptides prepared for the fluorescence studies was undetectable by thioflavin T (ThT) fluorescence.},
doi = {10.1002/chem.201804470},
journal = {Chemistry - A European Journal},
issn = {0947-6539},
number = 4,
volume = 25,
place = {United States},
year = {2018},
month = {11}
}

Journal Article:
Free Publicly Available Full Text
This content will become publicly available on November 9, 2019
Publisher's Version of Record

Save / Share: