Alies Bruno, Wiener Jacob D, Franz Katherine J
Department of Chemistry , Duke University , Durham , North Carolina 27708 , USA . Email:
Chem Sci. 2015 Jun 1;6(6):3606-3610. doi: 10.1039/c5sc00602c. Epub 2015 May 5.
A peptide has been designed so that its chelating affinity for one type of metal ion regulates its affinity for a second, different type of metal ion. The prochelator peptide (PCP), which is a fusion of motifs evocative of calcium loops and zinc fingers, forms a 1 : 2 Zn : peptide complex at pH 7.4 that increases its affinity for Zn ∼3-fold in the presence of Tb (log from 13.8 to 14.3), while the 1 : 1 luminescent complex with Tb is brighter, longer lived, and 20-fold tighter in the presence of Zn (log from 6.2 to 7.5). This unique example of cooperative, heterometallic allostery in a biologically compatible construct suggests the possibility of designing conditionally active metal-binding agents that could respond to dynamic changes in cellular metal status.
已设计出一种肽，使其对一种金属离子的螯合亲和力调节其对另一种不同类型金属离子的亲和力。前螯合剂肽（PCP）是钙环和锌指基序的融合体，在pH 7.4时形成1:2的锌-肽复合物，在铽存在的情况下，其对锌的亲和力增加约3倍（logK从13.8增加到14.3），而与铽形成的1:1发光复合物在锌存在时更亮、寿命更长且结合力增强20倍（logK从6.2增加到7.5）。这种在生物相容性构建体中协同、异金属变构的独特例子表明，有可能设计出能对细胞金属状态的动态变化做出反应的条件活性金属结合剂。
