Asakawa D, Osaka I
National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 2, 1-1-1 Umezono, Tsukuba, Ibaraki, 305-8568, Japan.
Center for Nano Materials and Technology, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Nomi, Ishikawa, 923-1211, Japan.
J Mass Spectrom. 2017 Feb;52(2):127-131. doi: 10.1002/jms.3906.
The ability of a thiol-containing molecule, thiosalicylic acid (TSA), to function as a reactive matrix for matrix-assisted laser desorption/ionization (MALDI) mass spectrometry analysis of peptides has been investigated. Although TSA has reducing characteristics, the use of TSA did not cause a reduction-induced MALDI in-source decay, probably because of the weak interactions between the thiol group in TSA and the carboxyl oxygen in the peptide. In contrast, when peptides containing disulfide bonds were analyzed by MALDI with TSA as the matrix, the disulfide bond was partially cleaved owing to the reaction with TSA, producing TSA-adducted peptides. The reaction between the disulfide bond and TSA was suggested to be occurred in solution. The comparison of the MALDI mass spectra obtained using conventional matrix and TSA allows us to count the number of disulfide bonds in the peptides. Copyright © 2017 John Wiley & Sons, Ltd.
已对含硫醇分子硫代水杨酸（TSA）作为肽的基质辅助激光解吸/电离（MALDI）质谱分析反应性基质的能力进行了研究。尽管TSA具有还原特性，但使用TSA并未导致还原诱导的MALDI源内衰变，这可能是因为TSA中的硫醇基团与肽中的羧基氧之间的相互作用较弱。相比之下，当以TSA为基质通过MALDI分析含二硫键的肽时，二硫键由于与TSA反应而部分断裂，产生TSA加合肽。二硫键与TSA之间的反应被认为发生在溶液中。使用传统基质和TSA获得的MALDI质谱的比较使我们能够计算肽中二硫键的数量。版权所有© 2017约翰威立父子有限公司。
