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Issue 3, 2014
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Investigating γ-secretase protein interactions in live cells using active site-directed clickable dual-photoaffinity probes

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Abstract

We have developed a suite of clickable γ-secretase active site-directed dual-photoaffinity probes possessing photoactivatable benzophenones that are located within the inhibitor scaffold as well as spaced away from the core by a linker. Through photoactivation of these dual photoprobes and subsequent click chemistry mediated conjugation of a reporter group, we have been able to specifically label PS1-N-terminal fragment (PS1-NTF), PS1-C-terminal fragment (PS1-CTF) and nicastrin and form a pseudo-full length PS1 through crosslinks between PS1-NTF and PS1-CTF. Probe-mediated protein–protein crosslinks were confirmed by in-gel fluorescence, western blotting and LC-MS/MS detection of tryptic peptides of the electrophoretically separated proteins.

Graphical abstract: Investigating γ-secretase protein interactions in live cells using active site-directed clickable dual-photoaffinity probes

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Supplementary files

Article information


Submitted
30 Sep 2013
Accepted
31 Oct 2013
First published
04 Nov 2013

Med. Chem. Commun., 2014,5, 321-327
Article type
Concise Article

Investigating γ-secretase protein interactions in live cells using active site-directed clickable dual-photoaffinity probes

T. E. Ballard, H. E. Murrey, K. F. Geoghegan, C. W. am Ende and D. S. Johnson, Med. Chem. Commun., 2014, 5, 321
DOI: 10.1039/C3MD00283G

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