Work

Parahydrogen Polarization in Reverse Micelles and Application to Sensing of Protein–Ligand Binding

Year: 2024

Type: article

Abstract: High Resolution Image Download MS PowerPoint Slide A medium containing reverse micelles supports non-hydrogenative parahydrogen induced polarization (nhPHIP) in the organic phase while solubilizing a protein in the aqueous phase. Strongly enhanced NMR signals from iridium hydride complexes report on a ligand, 4-amino-2-benzylaminopyrimidine, which crosses the phase boundary and interacts with the thiaminase protein TenA. The calculation of binding equilibria reveals a K D of 39.7 ± 8.9 μM for protein binding. The nanoscale separation of the two phases allows the separate optimization of the parahydrogen polarization and solubilization of a biological macromolecule. The reverse micelles may be used to study other biological questions using signal enhancement by parahydrogen polarization, such as enzyme reactions, protein–protein interactions, and protein binding epitopes.

Source: Journal of the American Chemical Society

Authors: Pierce Pham, Oindrila Biswas, Christian Hilty

Institution: Texas A&M University

Language: English

Topic: Advanced NMR Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funders: National Science Foundation, Welch Foundation, Division of Chemistry

Awards: G1020944575, G2988109435, Characterization of Macromolecular Dynamics Using Para-hydrogen Induced Polarization of Nuclear Spins