Another approach to protons with constricted mobility in white matter: pilot studies using wideline and high-resolution NMR spectroscopy.

We report a new approach for the identification of an independent method of studying the semi-solid pool of protons, i.e., protons with constrained motion as a result of being bound to lipid and protein matrices. These protons cannot be observed using conventional imaging techniques since their transverse relaxation times are much shorter than the minimum echo times that are currently available on clinical scanners. In this pilot study, in vitro multicomponent transverse relaxation experiments were made on human white matter slices, fixed in formalin (7 normal and 5 with multiple sclerosis). The transverse relaxation decay curves were multiexponential and were decomposed to yield three primary components. The shortest T(2) component that we obtained (a component too short to be seen by in vivo methods) was of the order of microseconds. We hypothesize that this might correspond to the macromolecular pool of lipid protons trapped within the myelin sheaths. To our knowledge, this is the first attempt at extracting this ultra short T(2) component from human white matter. Subsequently, an attempt was made to directly detect the lipid protons in a proton NMR spectrum and, if possible, measure their concentration in some of the tissues, using the technique of magic angle spinning.