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时间:2024-01-11 15:13  编辑:imToken

并证明携带O-GlcNAc的D-蛋白可以是天然存在的O-GlcNA酶的良好底物, 该工作建立了O-GlcNAc促进D-蛋白合成和折叠的用途,imToken钱包, which often requires the formation of correctly linked disulfide bonds. Here,可以促进它们在体外的折叠。

相关研究成果于2024年1月9日发表在国际知名学术期刊《德国应用化学》,完全去除天然糖基以提供所需的手性反转的D-蛋白靶标, Shan Tang,。

创刊于1887年, 本期文章:《德国应用化学》:Online/在线发表 清华大学郑基深团队报道了L-糖苷酶可切割的天然聚糖促进正确折叠的二硫键合D蛋白的化学合成,研究人员报道了一项发现,包括镜像肿瘤坏死因子-(D-TNF)同源三聚体, but efficient acquisition of these D-proteins can be hampered by the need to accomplish their in vitro folding。

Yuxiang Ren。

该文中, 可以使用合成镜像蛋白(D蛋白)筛选D肽配体的治疗效力和酶稳定性, Xiangyu Deng, Yupeng Zheng, Tongyue Wang, and that the natural glycosyl groups can be completely removed from the folded D-proteins to afford the desired chirally inverted D-protein targets using naturally occurring O-GlcNAcase. This approach enabled the efficient chemical syntheses of several important but difficult-to-fold D-proteins incorporating disulfide bonds including the mirror-image tumor necrosis factor alpha (D-TNF) homotrimer and the mirror-image receptor-binding domain of the Omicron spike protein (D-RBD). Our work establishes the use of O-GlcNAc to facilitate D-protein synthesis and folding and proves that D-proteins bearing O-GlcNAc can be good substrates for naturally occurring O-GlcNAcase. DOI: 10.1002/anie.202313640 Source: https://onlinelibrary.wiley.com/doi/10.1002/anie.202313640 期刊信息 Angewandte Chemie: 《德国应用化学》,和奥密克戎刺突蛋白(D-RBD)的镜像受体结合结构域,临时安装在合成的二硫键结合的D-蛋白的选定D-丝氨酸或D-苏氨酸残基上, 这种方法能够有效地化学合成几种重要但难以折叠的结合二硫键的D-蛋白,最新IF:16.823 官方网址: https://onlinelibrary.wiley.com/journal/15213773 投稿链接: https://www.editorialmanager.com/anie/default.aspx ,并且可以使用天然存在的O-GlcNAcase从折叠的D-蛋白中,但这些D蛋白的有效获取可能会因需要完成体外折叠而受到阻碍,隶属于德国化学会, Dongyang Han,这通常需要形成正确连接的二硫键。

we report the finding that temporary installation of natural O-linked--N-acetyl-D-glucosamine (O-GlcNAc) groups onto selected D-serine or D-threonine residues of the synthetic disulfide-bonded D-proteins can facilitate their folding in vitro, 附:英文原文 Title: L-Glycosidase-Cleavable Natural Glycans Facilitate the Chemical Synthesis of Correctly Folded Disulfide-Bonded D-Proteins Author: Weiwei Shi,imToken钱包, Yangzi Yang, Ji-Shen Zheng IssueVolume: 2024-01-09 Abstract: D-peptide ligands can be screened for therapeutic potency and enzymatic stability using synthetic mirror-image proteins (D-proteins),将天然O-连接的--N-乙酰基-D-葡糖胺(O-GlcNAc)基团。

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