Magnetic resonance water proton relaxation in protein solutions and tissue: T(1rho) dispersion characterization.


Autoria(s): Chen, EL; Kim, RJ
Data(s)

05/01/2010

Identificador

http://www.ncbi.nlm.nih.gov/pubmed/20052404

PLoS One, 2010, 5 (1), pp. e8565 - ?

http://hdl.handle.net/10161/4518

1932-6203

http://hdl.handle.net/10161/4518

Idioma(s)

ENG

en_US

Relação

PLoS One

10.1371/journal.pone.0008565

Plos One

Tipo

Journal Article

Cobertura

United States

Resumo

BACKGROUND: Image contrast in clinical MRI is often determined by differences in tissue water proton relaxation behavior. However, many aspects of water proton relaxation in complex biological media, such as protein solutions and tissue are not well understood, perhaps due to the limited empirical data. PRINCIPAL FINDINGS: Water proton T(1), T(2), and T(1rho) of protein solutions and tissue were measured systematically under multiple conditions. Crosslinking or aggregation of protein decreased T(2) and T(1rho), but did not change high-field T(1). T(1rho) dispersion profiles were similar for crosslinked protein solutions, myocardial tissue, and cartilage, and exhibited power law behavior with T(1rho)(0) values that closely approximated T(2). The T(1rho) dispersion of mobile protein solutions was flat above 5 kHz, but showed a steep curve below 5 kHz that was sensitive to changes in pH. The T(1rho) dispersion of crosslinked BSA and cartilage in DMSO solvent closely resembled that of water solvent above 5 kHz but showed decreased dispersion below 5 kHz. CONCLUSIONS: Proton exchange is a minor pathway for tissue T(1) and T(1rho) relaxation above 5 kHz. Potential models for relaxation are discussed, however the same molecular mechanism appears to be responsible across 5 decades of frequencies from T(1rho) to T(1).

Formato

e8565 - ?

Palavras-Chave #Animals #Electrophoresis, Polyacrylamide Gel #Hydrogen-Ion Concentration #Magnetic Resonance Imaging #Models, Theoretical #Proteins #Protons #Rabbits #Rats #Rats, Sprague-Dawley #Water