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Citation

BibTex format

@article{Lanyon-Hogg:2019:10.1039/C9SC01785B,
author = {Lanyon-Hogg, T and Ritzefeld, M and Sefer, L and Bickel, JK and Rudolf, A and Panyain, N and Bineva-Todd, G and Ocasio, C and OReilly, N and Siebold, C and Magee, AI and Tate, E},
doi = {10.1039/C9SC01785B},
journal = {Chemical Science},
pages = {8995--9000},
title = {Acylation-coupled lipophilic induction of polarisation (Acyl-cLIP): a universal assay for lipid transferase and hydrolase enzymes},
url = {http://dx.doi.org/10.1039/C9SC01785B},
volume = {10},
year = {2019}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Posttranslational attachment of lipids to proteins is important for many cellular functions, and the enzymes responsible for these modifications are implicated in many diseases, from cancer to neurodegeneration. Lipid transferases and hydrolases are increasingly tractable therapeutic targets, but present unique challenges for high-throughput biochemical enzyme assays which hinder development of new inhibitors. We present Acylation-coupled Lipophilic Induction of Polarisation (Acyl-cLIP) as the first universally applicable biochemical lipidation assay, exploiting the hydrophobic nature of lipidated peptides to drive a polarised fluorescence readout. Acyl-cLIP allows sensitive, accurate, real-time measurement of S- or N-palmitoylation, N-myristoylation, S-farnesylation or S-geranylgeranylation. Furthermore, it is applicable to transfer and hydrolysis reactions, and we demonstrate its extension to a high-throughput screening format. We anticipate that Acyl-cLIP will greatly expedite future drug discovery efforts against these challenging targets.
AU - Lanyon-Hogg,T
AU - Ritzefeld,M
AU - Sefer,L
AU - Bickel,JK
AU - Rudolf,A
AU - Panyain,N
AU - Bineva-Todd,G
AU - Ocasio,C
AU - OReilly,N
AU - Siebold,C
AU - Magee,AI
AU - Tate,E
DO - 10.1039/C9SC01785B
EP - 9000
PY - 2019///
SN - 2041-6520
SP - 8995
TI - Acylation-coupled lipophilic induction of polarisation (Acyl-cLIP): a universal assay for lipid transferase and hydrolase enzymes
T2 - Chemical Science
UR - http://dx.doi.org/10.1039/C9SC01785B
UR - http://hdl.handle.net/10044/1/71622
VL - 10
ER -