HPLC Purification of TRPM8 and Experimental Confirmation of Its Cholesterol Affinity on Synthetic Lipid Raft-like Models.

Clotilde Beatrice Angelucci, Annalaura Sabatucci, Alexandrine Kurtz, Davide Laurenti, Beatrice Dufrusine, Enrico Dainese, Antonio Francioso

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Article in Life (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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7 authors.

Clotilde Beatrice AngelucciDepartment of Veterinary Medicine, University of Teramo, 64100 Teramo, Italy.

Annalaura SabatucciDepartment of Bioscience and Technology for Food, Agriculture and Environment, University of Teramo, 64100 Teramo, Italy.ORCID 0000-0002-8004-2547

Alexandrine KurtzDepartment of Bioscience and Technology for Food, Agriculture and Environment, University of Teramo, 64100 Teramo, Italy.

Davide LaurentiDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, 00185 Rome, Italy.ORCID 0009-0008-1148-5898

Beatrice DufrusineDepartment of Bioscience and Technology for Food, Agriculture and Environment, University of Teramo, 64100 Teramo, Italy.ORCID 0000-0001-7515-9794

Enrico DaineseDepartment of Bioscience and Technology for Food, Agriculture and Environment, University of Teramo, 64100 Teramo, Italy.ORCID 0000-0001-7163-9344

Antonio FranciosoDepartment of Bioscience and Technology for Food, Agriculture and Environment, University of Teramo, 64100 Teramo, Italy.ORCID 0000-0001-9822-0260

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6 · The paper itself

Abstract

This study presents the successful expression, purification, and functional characterization of the human TRPM8 ion channel, a key player in temperature sensing and pain modulation. Using a modified bacterial expression protocol and DDM-based solubilization, TRPM8 was purified via HPLC-SEC and analyzed for its membrane-binding properties. FRET-based assays with synthetic lipid rafts revealed a strong and selective affinity of TRPM8 for cholesterol-containing membranes, suggesting cholesterol's role in modulating TRPM8 localization and activity. These findings provide quantitative in vitro evidence of TRPM8-cholesterol interactions and establish a robust model system for future structural and functional studies of membrane-associated proteins.

Indexed as

cholesterolFRETHPLC-SECion channellipid raftsTRPM8

Identifiers

PMID41900913

DOI10.3390/life16030392

PMCPMC13028388

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