Dataset Information

Membrane mimetic thermal proteome profiling (MM-TPP) towards mapping membrane protein-ligand dynamics

ABSTRACT: We combine the membrane mimetic (MM) Peptidisc with thermal proteome profiling (TPP) to screen membrane proteomes in detergent-free environments. Using whole mouse liver, we demonstrate the stabilization of integral membrane proteins (IMPs), specifically ATP-binding cassette transporters, through interactions with ATP and orthovanadate. Additionally, we assess the downstream effects of ATP hydrolysis products on IMP stability, such as that of GPCR purinergic receptors, and validate novel interactions with AlphaFold3

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli Mus Musculus (mouse)

TISSUE(S): Liver

SUBMITTER: Rupinder Jandu

LAB HEAD: Franck Duong van Hoa

PROVIDER: PXD055093 | Pride | 2025-11-17

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	DeamidationNQSites.txt	Txt
	DeamidationNQSitesE.txt	Txt
	DeamidationNQSitesL2.txt	Txt
	DeamidationNQSitesL3.txt	Txt
	HA230523_OE2_BN8155-15_1_RTL_NOTAG_NODETERGENT.index	Other

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Publications

Membrane-mimetic thermal proteome profiling (MM-TPP) toward mapping membrane protein-ligand dynamic interactions.

Jandu Rupinder Singh RS Bhattacharya Ashim A Antony Frank F Al-Seragi Mohammed M Aoki Hiroyuki H Babu Mohan M Duong van Hoa Franck F

eLife 20251112

Integral membrane proteins (IMPs) are central targets for small-molecule therapeutics, yet robust, unbiased, and detergent-free approaches to assess their on- and off-target interactions remain limited. Previously, we introduced the Peptidisc membrane mimetic (MM) for water-soluble stabilization of the membrane proteome and interactome (Carlson et al., eLife, 2019). In this work, we combine the Peptidisc with thermal proteome profiling (TPP) to establish membrane-mimetic thermal proteome profili ...[more]

PMID: 41223077

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