New method for site-specific modification of liposomes with proteins using sortase A-mediated transpeptidation.
New method for site-specific modification of liposomes with proteins using sortase A-mediated transpeptidation.
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使用分子酶A介导的转换的蛋白质对脂质体进行特定位点特异性修饰的新方法。
DOI：
10.1021/bc200694t
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发表时间：
2012-03-21
影响因子：
4.7
通讯作者：
Guo, Zhongwu
中科院分区：
文献类型：
--
作者：
Guo, Xueqing;Wu, Zhimeng;Guo, Zhongwu
建立了一种利用分选酶A（SrtA）介导的转肽反应对脂质体进行位点特异性修饰的新方法。在这方面，增强型绿色荧光蛋白（eGFP）被生物工程化以在其多肽C-末端携带由SrtA识别的LPATG基序，并用作连接至脂质体的蛋白质供体，所述脂质体用携带作为另一SrtA底物的双甘氨酸基序和eGFP受体的磷脂修饰。在SrtA的影响下，通过分析酶促反应产物和所得的荧光脂质体证明了eGFP有效地附着到脂质体上。结果表明，增加脂质体表面双甘氨酸基序的浓度和距离可以显著提高蛋白质修饰脂质体的效率。预期该策略可广泛用于其它蛋白质对脂质体的修饰。
A new method was developed for site-specific modifications of liposomes by proteins via sortase A (SrtA)-mediated transpeptidation reactions. In this regard, the enhanced green fluorescent protein (eGFP) was biologically engineered to carry at its polypeptide C-terminus the LPATG motif recognized by SrtA and used as the protein donor for linking to liposomes that were decorated with phospholipids carrying a diglycine motif as the other SrtA substrate and the eGFP acceptor. Under the influence of SrtA, eGFP was efficiently attached to liposomes, as proved by analyzing the enzymatic reaction products and the resultant fluorescent liposomes. It was observed that increasing the concentration and the distance of the diglycine motif on and from the liposome surface could significantly improve the efficiency of liposome modification by proteins. It is anticipated that this strategy can be widely useful for the modification of liposomes by other proteins.
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