封面：sac7d衍生的IgG fc特异性粘附蛋白的工程和结构解析及其在抗体光控亲和纯化中的应用（ChemBioChem 11/2025）

IF 2.6 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

ChemBioChem Pub Date : 2025-06-04 DOI:10.1002/cbic.202581101

Felix Veitl, Andreas Eichinger, Peter Mayrhofer, Markus R. Anneser, Mauricio Testanera, Kilian Rauscher, Matthias Lenz, Arne Skerra

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引用次数: 0

摘要

抗体（mab）是在生理条件下，通过光控亲和纯化，利用Sac7d支架和偶氮标记衍生的亲和力，从而克服了传统的蛋白A层析和酸触发洗脱的局限性一步分离出来的。x射线晶体学分析和亲和测量显示，在CH2/CH3连接处与Fc形成复合物，类似于蛋白A/G和FnRn，该复合物远离结合位点，因此可以直接将纯化的mAb用于生化或细胞培养分析。更多细节可以在Arne Skerra及其同事的文章2500102中找到。

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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Front Cover: Engineering and Structural Elucidation of a Sac7d-Derived IgG Fc-Specific Affitin and Its Application for the Light-Controlled Affinity Purification of Antibodies (ChemBioChem 11/2025)

Antibodies (mAbs) are isolated in one step, under physiological conditions, via light-controlled affinity purification using an affitin derived from the Sac7d scaffold and the Azo-tag, thus overcoming limitations of conventional protein A chromatography and acid-triggered elution. X-ray crystallographic analysis and affinity measurements revealed complex formation of the affitin with Fc at the C_H2/C_H3 junction, similar to protein A/G and FnRn, which is remote from the binding site, hence allowing direct application of the purified mAb for biochemical or cell culture assays. More details can be found in article 2500102 by Arne Skerra and co-workers.

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来源期刊

ChemBioChem 生物-生化与分子生物学

CiteScore

6.10

自引率

3.10%

发文量

407

审稿时长

1 months

期刊介绍： ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).