Cover Feature: Sulfoxide-Mediated Cys-Trp-Selective Bioconjugation that Enables Protein Labeling and Peptide Heterodimerization (ChemistryEurope 3-4/2024)

ChemistryEurope Pub Date : 2024-07-08 DOI:10.1002/ceur.202400047

Dr. Daishiro Kobayashi, Dr. Masaya Denda, Junya Hayashi, Kota Hidaka, Yutaka Kohmura, Dr. Takaaki Tsunematsu, Dr. Kohei Nishino, Dr. Harunori Yoshikawa, Dr. Kento Ohkawachi, Dr. Kiyomi Nigorikawa, Dr. Tetsuro Yoshimaru, Prof. Naozumi Ishimaru, Prof. Wataru Nomura, Prof. Toyomasa Katagiri, Prof. Hidetaka Kosako, Prof. Akira Otaka

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Abstract

A tryptophan modification that utilizes S-acetamidomethyl cysteine sulfoxide under mildly acidic conditions with magnesium chloride was achieved. An optimum condition in an ionic liquid allowed antibody modification without significant denaturation. In their Research Article, A. Otaka and co-workers describe the difference in chemical behaviors to acids between S-acetamidomethyl and p-methoxybenzyl cysteine sulfoxides permitted peptide heterodimerization in a one-pot sequential manner.

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封面专题：过氧化硫介导的 Cys-Trp 选择性生物键合可实现蛋白质标记和多肽异源二聚化（欧洲化学 3-4/2024 期）

在氯化镁的弱酸性条件下，利用 S-乙酰胺甲基半胱氨酸亚砜对色氨酸进行了修饰。在离子液体中的最佳条件下，抗体修饰不会发生明显变性。在他们的研究文章中，A. Otaka 及其合作者描述了 S-乙酰胺基甲基半胱氨酸亚砜和对甲氧基苄基半胱氨酸亚砜对酸的化学行为差异，这使得肽异二聚化可以以一锅顺序的方式进行。

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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ChemistryEurope

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