Last-Step Enzymatic [(18) F]-Fluorination of Cysteine-Tethered RGD Peptides Using Modified Barbas Linkers.
Last-Step Enzymatic [(18) F]-Fluorination of Cysteine-Tethered RGD Peptides Using Modified Barbas Linkers.
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DOI：
10.1002/chem.201601361
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发表时间：
2016-07
期刊：
影响因子：
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通讯作者：
Qing-zhi Zhang;S. Dall’Angelo;I. Fleming;L. Schweiger;M. Zanda;D. O'Hagan
中科院分区：
文献类型：
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作者：
Qing-zhi Zhang;S. Dall’Angelo;I. Fleming;L. Schweiger;M. Zanda;D. O'Hagan
我们报道了含半胱氨酸的RGD肽的最后一步氟化酶催化[(18)F]-氟化。该肽通过硫连接到最近发现的Barbas连接体的一个修饰的更亲水的变体上，Barbas连接体本身通过聚乙二醇链连接到氯腺苷部分。氟酶能够利用该结构体作为底物进行转绿原化反应，生成[(18)F]-放射性标记的RGD肽，该肽与癌细胞相关的αv β3整合素保持高亲和力。
We report a last-step fluorinase-catalyzed [(18) F]-fluorination of a cysteine-containing RGD peptide. The peptide was attached through sulfur to a modified and more hydrophilic variant of the recently disclosed Barbas linker which was itself linked to a chloroadenosine moiety via a PEGylated chain. The fluorinase was able to use this construct as a substrate for a transhalogenation reaction to generate [(18) F]-radiolabeled RGD peptides, which retained high affinity to cancer-cell relevant αv β3 integrins.