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Mechanism of magnetization transfer during on‐resonance water saturation. A new approach to detect mobile proteins, peptides, and lipids
Author(s) -
van Zijl Peter C.M.,
Zhou Jinyuan,
Mori Noriko,
Payen JeanFrancois,
Wilson David,
Mori Susumu
Publication year - 2003
Publication title -
magnetic resonance in medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.696
H-Index - 225
eISSN - 1522-2594
pISSN - 0740-3194
DOI - 10.1002/mrm.10398
Subject(s) - magnetization transfer , chemistry , macromolecule , proton , amide , intramolecular force , magnetization , nuclear overhauser effect , nuclear magnetic resonance , proton nmr , nuclear magnetic resonance spectroscopy , biophysics , stereochemistry , biochemistry , magnetic resonance imaging , medicine , physics , quantum mechanics , biology , magnetic field , radiology
Abstract The mechanism of magnetization transfer (MT) between water and components of the proton spectrum was studied ex vivo in a perfused cell system and in vivo in the rat brain (n = 5). Water was selectively labeled and spectral buildup consequential to transfer of longitudinal magnetization was followed as a function of time. At short mixing time ( T m ), nitrogen‐bound solvent‐exchangeable protons were observed, predominantly assigned to amide groups of proteins and peptides. At longer T m , intramolecular nuclear Overhauser enhancement (NOE) was observed in the aliphatic proton region, leading to a mobile‐macromolecule‐weighted spectrum that resembles typical protein spectra described in the literature. This effect on the proton spectrum is distinct from that of classical off‐resonance MT, which has been shown to be due to the immobile solid‐like proton pool. When studying a solution of major brain metabolites under physiological concentrations and conditions (pH), no transfer effects were observed, in line with expectations based on reduced NOE effects in rapidly tumbling molecules and the fast proton exchange rates of amino, amine, SH, and OH groups. The spectral intensities of the amide protons may serve as indicators for pH and cellular levels of mobile proteins and peptides, while the aliphatic components are representative of several types of mobile macromolecules, including proteins, peptides, and lipids. Magn Reson Med 49:440–449, 2003. © 2003 Wiley‐Liss, Inc.