Proteomics

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Chemoproteomic target deconvolution of Lipoic acid reveals Histone Deacetylases as the main targets

ABSTRACT: Here we set out to identify protein targets of Lipoic acid and Lipoamide by chemical proteomics approaches. We generated Lipoamide-based affinity matrices to pulldown target proteins and quantify them via bottom-up proteomics. Use of the same affinity matrix in dose dependent compeition assays allowed us to identify HDACs as potently bound by Lipoic acid and Lipoamide and to derive the affinty of drug target interactions. These findings were confirmed by further competiiton assays with already established HDAC inhibitor based affinity matrices.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Severin Lechner  

LAB HEAD: Bernhard Kuster

PROVIDER: PXD036810 | Pride | 2026-06-02

REPOSITORIES: Pride

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LipoAmide_vs_iL_in_MV411_raw.zip Other
LipoAmide_vs_iL_in_MV411_txt.zip Other
LipoAmide_vs_iL_in_SW620_raw.zip Other
LipoAmide_vs_iL_in_SW620_txt.zip Other
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Chemoproteomic target deconvolution reveals Histone Deacetylases as targets of (R)-lipoic acid.

Lechner Severin S   Steimbach Raphael R RR   Wang Longlong L   Deline Marshall L ML   Chang Yun-Chien YC   Fromme Tobias T   Klingenspor Martin M   Matthias Patrick P   Miller Aubry K AK   Médard Guillaume G   Kuster Bernhard B  

Nature communications 20230615 1

Lipoic acid is an essential enzyme cofactor in central metabolic pathways. Due to its claimed antioxidant properties, racemic (R/S)-lipoic acid is used as a food supplement but is also investigated as a pharmaceutical in over 180 clinical trials covering a broad range of diseases. Moreover, (R/S)-lipoic acid is an approved drug for the treatment of diabetic neuropathy. However, its mechanism of action remains elusive. Here, we performed chemoproteomics-aided target deconvolution of lipoic acid a  ...[more]

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