Consequences of 129Xe–1H Cross Relaxation in Aqueous Solutions

Abstract

We have investigated the transfer of polarization from 129Xe to solute protons in aqueous solutions to determine the feasibility of using hyperpolarized xenon to enhance 1H sensitivity in aqueous systems at or near room temperatures. Several solutes, each of different molecular weight, were dissolved in deuterium oxide and although large xenon polarizations were created, no significant proton signal enhancement was detected in l-tyrosine, α-cyclodextrin, β-cyclodextrin, apomyoglobin, or myoglobin. Solute-induced enhancement of the 129Xe spin–lattice relaxation rate was observed and depended on the size and structure of the solute molecule. The significant increase of the apparent spin–lattice relaxation rate of the solution phase 129Xe by α-cyclodextrin and apomyoglobin indicates efficient cross relaxation. The slow relaxation of xenon in β-cyclodextrin and l-tyrosine indicates weak coupling and inefficient cross relaxation. Despite the apparent cross-relaxation effects, all attempts to detect the proton enhancement directly were unsuccessful. Spin–lattice relaxation rates were also measured for Boltzmann 129Xe in myoglobin. The cross-relaxation rates were determined from changes in 129Xe relaxation rates in the α-cyclodextrin and myoglobin solutions. These cross-relaxation rates were then used to model 1H signal gains for a range of 129Xe to 1H spin population ratios. These models suggest that in spite of very large 129Xe polarizations, the 1H gains will be less than 10% and often substantially smaller. In particular, dramatic 1H signal enhancements in lung tissue signals are unlikely.