ArticleJournal of nanobiotechnology2025
Lipid liquid-crystalline nanoparticles as a suitable platform for accommodating sensitive membrane proteins: monitoring the activity of HMG-CoA reductase.
Article in Journal of nanobiotechnology, 2025. 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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Abstract
Biological molecules such as integral membrane proteins, peptides, and nucleic acids that are not soluble or sufficiently stable in aqueous solutions can be stabilized through encapsulation in lipid nanoparticles. Discovering the potential of lipid liquid-crystalline nanoparticles opens up exciting possibilities for housing sensitive membrane proteins. Lipid mesophases provide an environment that protects the cargo, usually a drug, from rapid clearance or degradation. This study employed the mentioned platform to stabilize a different cargo-an essential transmembrane enzyme, HMG-CoA reductase (HMGR). The nanostructured lipid liquid-crystalline (LLC) nanoparticles known as hexosomes are selected as a convenient nanocontainer for the redox-active protein for real-time monitoring of its functions in the bulk of the solution and point to the applicability of the proposed platform in the evaluation of therapeutic functions of the protein by standard physicochemical methods. Instead of using detergents, which usually affect the functions and stability of sensitive membrane proteins, we provide a suitable environment, protecting them in the bulk of the solution against other present species, e.g., toxic compounds or degrading proteins. The objective was to optimize the composition and structure of the lipid nanoparticles to meet the needs of such sensitive and flexible membrane proteins as HMGR and compare the functioning of the encapsulated enzyme with that of the same protein free in the aqueous solution. The catalytic reaction of HMGR involves the 4-electron reduction of HMG-CoA to mevalonate and CoA while simultaneously oxidizing NADPH to NADP
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