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Enzymatic Installation of Functional Molecules on Amyloid-Based Polymers
Bioconjugate Chemistry ( IF 4.7 ) Pub Date : 2017-11-03 00:00:00 , DOI: 10.1021/acs.bioconjchem.7b00479
Tatsuki Ohshima 1 , Masafumi Sakono 1
Affiliation  

We produced a functional polymer whose framework comprised transthyretin (TTR) amyloid fibrils. In order to immobilize functional molecules onto the amyloid fibrils, transpeptidase sortase A (srtA), which catalyzes the covalent binding of LPXTG with polyglycine, was employed. After the preparation of the amyloid fibril of LPETGG-tagged TTR, immobilization of Gly5-fused GFP on the amyloid fibrils by srtA-mediated transpeptidation was carried out. SrtA recognized the amyloid fibrils consisting of an LPETGG-tagged TTR variant (L55P) as a good substrate, resulting in successful preparation of a GFP-immobilized amyloid. Intriguingly, the replacement of GFP with Gly5-fused luciferase was confirmed when the GFP-immobilized amyloids were mixed with Gly5-luciferase in the presence of srtA. Thus, it was found that functional molecules covalently immobilized on amyloid could be detached and substituted with other tagged molecules by using srtA.

中文翻译:

在基于淀粉样蛋白的聚合物上酶促功能分子的安装

我们生产了一种功能聚合物,其骨架包含运甲状腺素蛋白(TTR)淀粉样蛋白原纤维。为了将功能分子固定在淀粉样蛋白原纤维上,使用了催化LPXTG与聚甘氨酸共价结合的转肽酶分选酶A(srtA)。在制备经LPETGG标记的TTR的淀粉样蛋白原纤维后,通过srtA介导的转肽作用将Gly5融合的GFP固定在淀粉样蛋白原纤维上。SrtA认识到由LPETGG标记的TTR变体(L55P)组成的淀粉样蛋白原纤维是良好的底物,从而成功制备了GFP固定的淀粉样蛋白。有趣的是,当在srtA存在下,将固定有GFP的淀粉样蛋白与Gly5-荧光素酶混合时,证实了用Gly5融合的荧光素酶替代了GFP。因此,
更新日期:2017-11-03
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