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Volume 19
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10.3390/ijms19113682
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Communication

A Cysteine-Reactive Small Photo-Crosslinker Possessing Caged-Fluorescence Properties: Binding-Site Determination of a Combinatorially-Selected Peptide by Fluorescence Imaging/Tandem Mass Spectrometry

by
Kazuki Yatabe
†,
Masaru Hisada
†,
Yudai Tabuchi
and
Masumi Taki
*
Department of Engineering Science, Bioscience and Technology Program, The Graduate School of Informatics and Engineering, The University of Electro-Communications (UEC), 1-5-1 Chofugaoka, Chofu, Tokyo 182-8585, Japan
*
Author to whom correspondence should be addressed.
†
These authors contributed equally and are considered as co-first authors.
Int. J. Mol. Sci. 2018, 19(11), 3682; https://doi.org/10.3390/ijms19113682
Submission received: 28 September 2018 / Revised: 15 November 2018 / Accepted: 16 November 2018 / Published: 21 November 2018
(This article belongs to the Section Physical Chemistry and Chemical Physics)
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Abstract

To determine the binding-site of a combinatorially-selected peptide possessing a fluoroprobe, a novel cysteine reactive small photo-crosslinker that can be excited by a conventional long-wavelength ultraviolet handlamp (365 nm) was synthesized via Suzuki coupling with three steps. The crosslinker is rationally designed, not only as a bioisostere of the fluoroprobe, but as a caged-fluorophore, and the photo-crosslinked target protein became fluorescent with a large Stokes-shift. By introducing the crosslinker to a designated sulfhydryl (SH) group of a combinatorially-selected peptide, the protein-binding site of the targeted peptide was deduced by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)/fluorescence imaging followed by matrix-assisted laser desorption ionization-time of flight tandem mass spectrometry (MALDI-TOF-MS/MS) analysis.
Keywords: binding-site determination; combinatorially-selected peptide; caged fluorophore; pharmacophore; photoaffinity labeling (PAL); bioisostere; cysteine-reactive crosslinker; fluorescence imaging; tandem MS analysis; covalent binder binding-site determination; combinatorially-selected peptide; caged fluorophore; pharmacophore; photoaffinity labeling (PAL); bioisostere; cysteine-reactive crosslinker; fluorescence imaging; tandem MS analysis; covalent binder
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MDPI and ACS Style

Yatabe, K.; Hisada, M.; Tabuchi, Y.; Taki, M. A Cysteine-Reactive Small Photo-Crosslinker Possessing Caged-Fluorescence Properties: Binding-Site Determination of a Combinatorially-Selected Peptide by Fluorescence Imaging/Tandem Mass Spectrometry. Int. J. Mol. Sci. 2018, 19, 3682. https://doi.org/10.3390/ijms19113682

AMA Style

Yatabe K, Hisada M, Tabuchi Y, Taki M. A Cysteine-Reactive Small Photo-Crosslinker Possessing Caged-Fluorescence Properties: Binding-Site Determination of a Combinatorially-Selected Peptide by Fluorescence Imaging/Tandem Mass Spectrometry. International Journal of Molecular Sciences. 2018; 19(11):3682. https://doi.org/10.3390/ijms19113682

Chicago/Turabian Style

Yatabe, Kazuki, Masaru Hisada, Yudai Tabuchi, and Masumi Taki. 2018. "A Cysteine-Reactive Small Photo-Crosslinker Possessing Caged-Fluorescence Properties: Binding-Site Determination of a Combinatorially-Selected Peptide by Fluorescence Imaging/Tandem Mass Spectrometry" International Journal of Molecular Sciences 19, no. 11: 3682. https://doi.org/10.3390/ijms19113682

APA Style

Yatabe, K., Hisada, M., Tabuchi, Y., & Taki, M. (2018). A Cysteine-Reactive Small Photo-Crosslinker Possessing Caged-Fluorescence Properties: Binding-Site Determination of a Combinatorially-Selected Peptide by Fluorescence Imaging/Tandem Mass Spectrometry. International Journal of Molecular Sciences, 19(11), 3682. https://doi.org/10.3390/ijms19113682

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