Magnetic Resonance Water Proton Relaxation in Protein Solutions and Tissue: T1p Dispersion Characterization

被引:18
作者
Chen, Enn-Ling [1 ,2 ]
Kim, Raymond J. [1 ,2 ,3 ]
机构
[1] Duke Univ, Med Ctr, Duke Cardiovasc Magnet Resonance Ctr, Durham, NC 27706 USA
[2] Duke Univ, Med Ctr, Dept Med, Durham, NC 27710 USA
[3] Duke Univ, Med Ctr, Dept Radiol, Durham, NC 27710 USA
来源
PLOS ONE | 2010年 / 5卷 / 01期
关键词
SPIN-LATTICE-RELAXATION; PANCREATIC TRYPSIN-INHIBITOR; BOVINE SERUM-ALBUMIN; CROSS-RELAXATION; HETEROGENEOUS SYSTEMS; BIOPOLYMER SYSTEMS; AQUEOUS-SOLUTION; EXCHANGE; DYNAMICS; DEPENDENCE;
D O I
10.1371/journal.pone.0008565
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 T1, T2, and T-1p of protein solutions and tissue were measured systematically under multiple conditions. Crosslinking or aggregation of protein decreased T2 and T-1p, but did not change high-field T1, T-1p dispersion profiles were similar for crosslinked protein solutions, myocardial tissue, and cartilage, and exhibited power law behavior with T-1p(0) values that closely approximated T2. The T-1p 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-1p 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 T1 and T-1p 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-1p to T1.
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页数:12
相关论文
共 41 条
[1]  
[Anonymous], 2016, Primer of Applied Regression and Analysis of Variance
[2]   PRIMARY STRUCTURE EFFECTS ON PEPTIDE GROUP HYDROGEN-EXCHANGE [J].
BAI, YW ;
MILNE, JS ;
MAYNE, L ;
ENGLANDER, SW .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1993, 17 (01) :75-86
[3]   RELAXATION EFFECTS IN NUCLEAR MAGNETIC RESONANCE ABSORPTION [J].
BLOEMBERGEN, N ;
PURCELL, EM ;
POUND, RV .
PHYSICAL REVIEW, 1948, 73 (07) :679-712
[4]  
BOTTOMLEY PA, 1984, MED PHYS, V11, P425, DOI 10.1118/1.595535
[5]   1/T1-RHO AND LOW-FIELD 1/T1 OF TISSUE WATER PROTONS ARISE FROM MAGNETIZATION TRANSFER TO MACROMOLECULAR SOLID-STATE BROADENED LINES [J].
BROWN, RD ;
KOENIG, SH .
MAGNETIC RESONANCE IN MEDICINE, 1992, 28 (01) :145-152
[6]   THE MAGNETIC-FIELD DEPENDENCE OF PROTON SPIN RELAXATION IN TISSUES [J].
BRYANT, RG ;
MENDELSON, DA ;
LESTER, CC .
MAGNETIC RESONANCE IN MEDICINE, 1991, 21 (01) :117-126
[7]  
BRYANT RG, 1980, 178 M AM CHEM SOC WA
[8]   3-DIMENSIONAL STRUCTURE OF HUMAN-SERUM ALBUMIN [J].
CARTER, DC ;
HE, XM ;
MUNSON, SH ;
TWIGG, PD ;
GERNERT, KM ;
BROOM, MB ;
MILLER, TY .
SCIENCE, 1989, 244 (4909) :1195-1198
[9]   RESIDENCE TIMES OF THE BURIED WATER-MOLECULES IN BOVINE PANCREATIC TRYPSIN-INHIBITOR AND ITS G36S MUTANT [J].
DENISOV, VP ;
HALLE, B ;
PETERS, J ;
HORLEIN, HD .
BIOCHEMISTRY, 1995, 34 (28) :9046-9051
[10]   PROTEIN HYDRATION DYNAMICS IN AQUEOUS-SOLUTION - A COMPARISON OF BOVINE PANCREATIC TRYPSIN-INHIBITOR AND UBIQUITIN BY O-17 SPIN RELAXATION DISPERSION [J].
DENISOV, VP ;
HALLE, B .
JOURNAL OF MOLECULAR BIOLOGY, 1995, 245 (05) :682-697