甘露糖修饰α-螺旋肽噬菌体文库†中魔豆蛋白A结合物的筛选

IF 3.743 Q2 Biochemistry, Genetics and Molecular Biology

Molecular BioSystems Pub Date : 2017-09-13 DOI:10.1039/C7MB00495H

Iou Ven Chang, Hiroshi Tsutsumi and Hisakazu Mihara

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引用次数: 7

摘要

甘露糖修饰的凝集素结合肽从α-螺旋设计的肽噬菌体文库中获得。以ConA作为凝集素家族的代表性靶蛋白。所鉴定的糖肽能以微摩尔亲和力选择性地与ConA结合。基于这些结果，本研究中描述的方法将通过糖和肽单元的协同作用增强糖修饰配体的选择，对凝集素蛋白具有更好的特异性和亲和力。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Screening for concanavalin A binders from a mannose-modified α-helix peptide phage library†

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Screening for concanavalin A binders from a mannose-modified α-helix peptide phage library†

Mannose-modified lectin-binding peptides were obtained from an α-helical-designed peptide phage library. Concanavalin A (ConA) was used as a representative target protein for the lectin family. The identified glycopeptides could selectively bind to ConA with micromolar affinity. With these results, the methodologies described in this study will enhance the selection of saccharide-modified ligands through the synergistic effects of sugar and peptide units, with better specificity and affinity towards lectin proteins.

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来源期刊

Molecular BioSystems 生物-生化与分子生物学

CiteScore

2.94

自引率

0.00%

发文量

审稿时长

2.6 months

期刊介绍： Molecular Omics publishes molecular level experimental and bioinformatics research in the -omics sciences, including genomics, proteomics, transcriptomics and metabolomics. We will also welcome multidisciplinary papers presenting studies combining different types of omics, or the interface of omics and other fields such as systems biology or chemical biology.