通过一锅氰化法和 MALDI-TOF-MS/MS,对固定在单个珠子上的环肽进行高通量序列测定,以发现相互作用的肽。

IF 1.8 4区 化学 Q3 CHEMISTRY, ANALYTICAL Analytical Sciences Pub Date : 2024-05-22 DOI:10.1007/s44211-024-00594-8
Takeshi Kasama, Kiyoshi Nokihara
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引用次数: 0

摘要

固定在一个凝胶型微珠上的环肽已被用于发现相互作用的肽和/或药用中型分子。虽然识别肽的高通量表征一直是一个瓶颈,但在这里,我们介绍了通过使用 2-硝基-5-硫氰基苯甲酸的一锅反应直接将肽从珠子中释放出来,然后进行质谱分析,从而实现对珠子上的肽进行更快的常规测序。这有助于研究蛋白质与蛋白质之间的相互作用以及发现候选药物。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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A high-throughput sequence determination for one cyclic peptide immobilized on a single bead by the one-pot cyanidation followed by MALDI-TOF–MS/MS for discovery of interacting peptides

One cyclic peptide immobilized on one gel-type bead has been employed for the discovery of both interacting peptides and/or medicinal medium-sized molecules. Although high-throughput characterization of recognized peptides has been a bottleneck, here, we describe direct liberation from beads by a one-pot reaction using 2-nitro-5-thiocyanatobenzoic acid followed by mass spectrometry to realize faster and routine sequencing of the peptide on the beads. This is useful for the investigation of protein–protein interactions as well as discovery of drug candidates.

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来源期刊
Analytical Sciences
Analytical Sciences 化学-分析化学
CiteScore
2.90
自引率
18.80%
发文量
232
审稿时长
1 months
期刊介绍: Analytical Sciences is an international journal published monthly by The Japan Society for Analytical Chemistry. The journal publishes papers on all aspects of the theory and practice of analytical sciences, including fundamental and applied, inorganic and organic, wet chemical and instrumental methods. This publication is supported in part by the Grant-in-Aid for Publication of Scientific Research Result of the Japanese Ministry of Education, Culture, Sports, Science and Technology.
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