Murayama Chihiro, Kimura Yoshishige, Setou Mitsutoshi
Department of Molecular Anatomy, Molecular Imaging Frontier Research Center, Hamamatsu University School of Medicine, 1-20-1 Handayama, Higashi-ku, 431-3192, Hamamatsu, Shizuoka, Japan.
Biophys Rev. 2009 Sep;1(3):131. doi: 10.1007/s12551-009-0015-6. Epub 2009 Sep 9.
Imaging mass spectrometry (IMS) is two-dimensional mass spectrometry to visualize the spatial distribution of biomolecules, which does not need either separation or purification of target molecules, and enables us to monitor not only the identification of unknown molecules but also the localization of numerous molecules simultaneously. Among the ionization techniques, matrix assisted laser desorption/ionization (MALDI) is one of the most generally used for IMS, which allows the analysis of numerous biomolecules ranging over wide molecular weights. Proper selection and preparation of matrix is essential for successful imaging using IMS. Tandem mass spectrometry, which is referred to MS, enables the structural analysis of a molecule detected by the first step of IMS. Applications of IMS were initially developed for studying proteins or peptides. At present, however, targets of IMS research have expanded to the imaging of small endogenous metabolites such as lipids, exogenous drug pharmacokinetics, exploring new disease markers, and other new scientific fields. We hope that this new technology will open a new era for biophysics.
成像质谱(IMS)是一种二维质谱技术,用于可视化生物分子的空间分布,它既不需要对目标分子进行分离也不需要纯化,使我们不仅能够监测未知分子的鉴定,还能同时监测众多分子的定位。在电离技术中,基质辅助激光解吸/电离(MALDI)是IMS最常用的技术之一,它允许分析分子量范围广泛的众多生物分子。正确选择和制备基质对于使用IMS成功成像至关重要。串联质谱,简称MS,能够对IMS第一步检测到的分子进行结构分析。IMS的应用最初是为研究蛋白质或肽而开发的。然而,目前IMS研究的目标已经扩展到对脂质等内源性小分子代谢物的成像、外源性药物的药代动力学、探索新的疾病标志物以及其他新的科学领域。我们希望这项新技术将为生物物理学开启一个新时代。