De Novo Sequencing of Peptides on Single Resin Beads by MALDI-FTICR Tandem Mass Spectrometry
De Novo Sequencing of Peptides on Single Resin Beads by MALDI-FTICR Tandem Mass Spectrometry
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DOI：
10.1016/j.jasms.2009.10.004
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发表时间：
2010-02-01
影响因子：
3.2
通讯作者：
Wittmann, Valentin
中科院分区：
文献类型：
--
作者：
Semmler, Angelika;Weber, Reinhold;Wittmann, Valentin
组合化学中的一种有效方法是合成一珠一化合物肽库。与以大部分自动化方式进行的合成和功能筛选相比，结构测定经常是费力和耗时的。在这里，我们报告了一种方法从头测序的肽在单珠基质辅助激光解吸/电离傅里叶变换离子回旋共振（MALDI-FTICR）串联质谱法，使用的树脂与光链接固相肽合成。在分选出单个珠后，开发了MALDI靶上的有效样品制备，其能够在用紫外（UV）-MALDI激光照射珠-基质混合物时进行碎片化，在增加的激光能量下具有序列特异性碎片离子的提高的产率。这种方法是由两个肽的序列测定从一个单一的氨基酸序列不同的图书馆，串联MS程序和碎片离子分配的可行性进行了确认，通过持续的非共振辐射/碰撞诱导解离（SORI/CID）和红外多光子解离（IRMPD）碎片。（J Am Soc Mass Spectrom 2010，21，215-219）（C）2010由Elsevier Inc.美国质谱学会American Society for Mass Spectrometry
An efficient approach in combinatorial chemistry is the synthesis of one-bead-one-compound peptide libraries. In contrast to synthesis and functional screening, which is performed in a largely automated manner, structure determination has been frequently laborious and time-consuming. Here we report an approach for de novo sequencing of peptides on single beads by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance (MALDI-FTICR) tandem mass spectrometry, using a resin with a photolinker for solid-phase peptide synthesis. Upon sorting out single beads, an efficient sample preparation on the MALDI target was developed that enables fragmentation upon irradiation of the bead-matrix mixture with the ultraviolet (UV)-MALDI laser, with enhanced yield of sequence-specific fragment ions at increased laser energy. This approach is illustrated by sequence determinations of two peptides from a library with sequences varying in a single amino acid; the feasibility with tandem-MS procedures and fragment ion assignment was ascertained by sustained off-resonance irradiation/collision induced dissociation (SORI/CID) and infrared multiphoton dissociation (IRMPD) fragmentation. (J Am Soc Mass Spectrom 2010, 21, 215-219) (C) 2010 Published by Elsevier Inc. on behalf of American Society for Mass Spectrometry