Cargando…
Magnetic Resonance Water Proton Relaxation in Protein Solutions and Tissue: T(1ρ) Dispersion Characterization
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 d...
Autores principales: | , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2797329/ https://www.ncbi.nlm.nih.gov/pubmed/20052404 http://dx.doi.org/10.1371/journal.pone.0008565 |
_version_ | 1782175604881227776 |
---|---|
author | Chen, Enn-Ling Kim, Raymond J. |
author_facet | Chen, Enn-Ling Kim, Raymond J. |
author_sort | Chen, Enn-Ling |
collection | PubMed |
description | 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(1ρ) of protein solutions and tissue were measured systematically under multiple conditions. Crosslinking or aggregation of protein decreased T(2) and T(1ρ), but did not change high-field T(1). T(1ρ) dispersion profiles were similar for crosslinked protein solutions, myocardial tissue, and cartilage, and exhibited power law behavior with T(1ρ)(0) values that closely approximated T(2). The T(1ρ) 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(1ρ) 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(1ρ) 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(1ρ) to T(1). |
format | Text |
id | pubmed-2797329 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-27973292010-01-06 Magnetic Resonance Water Proton Relaxation in Protein Solutions and Tissue: T(1ρ) Dispersion Characterization Chen, Enn-Ling Kim, Raymond J. PLoS One Research Article 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(1ρ) of protein solutions and tissue were measured systematically under multiple conditions. Crosslinking or aggregation of protein decreased T(2) and T(1ρ), but did not change high-field T(1). T(1ρ) dispersion profiles were similar for crosslinked protein solutions, myocardial tissue, and cartilage, and exhibited power law behavior with T(1ρ)(0) values that closely approximated T(2). The T(1ρ) 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(1ρ) 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(1ρ) 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(1ρ) to T(1). Public Library of Science 2010-01-05 /pmc/articles/PMC2797329/ /pubmed/20052404 http://dx.doi.org/10.1371/journal.pone.0008565 Text en Chen, Kim. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Chen, Enn-Ling Kim, Raymond J. Magnetic Resonance Water Proton Relaxation in Protein Solutions and Tissue: T(1ρ) Dispersion Characterization |
title | Magnetic Resonance Water Proton Relaxation in Protein Solutions and Tissue: T(1ρ) Dispersion Characterization |
title_full | Magnetic Resonance Water Proton Relaxation in Protein Solutions and Tissue: T(1ρ) Dispersion Characterization |
title_fullStr | Magnetic Resonance Water Proton Relaxation in Protein Solutions and Tissue: T(1ρ) Dispersion Characterization |
title_full_unstemmed | Magnetic Resonance Water Proton Relaxation in Protein Solutions and Tissue: T(1ρ) Dispersion Characterization |
title_short | Magnetic Resonance Water Proton Relaxation in Protein Solutions and Tissue: T(1ρ) Dispersion Characterization |
title_sort | magnetic resonance water proton relaxation in protein solutions and tissue: t(1ρ) dispersion characterization |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2797329/ https://www.ncbi.nlm.nih.gov/pubmed/20052404 http://dx.doi.org/10.1371/journal.pone.0008565 |
work_keys_str_mv | AT chenennling magneticresonancewaterprotonrelaxationinproteinsolutionsandtissuet1rdispersioncharacterization AT kimraymondj magneticresonancewaterprotonrelaxationinproteinsolutionsandtissuet1rdispersioncharacterization |