Hydrolytically active Eu(III) and Ce(IV) EF-hand peptides
Hydrolytically active Eu(III) and Ce(IV) EF-hand peptides
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DOI：
10.1016/s0162-0134(02)00408-7
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发表时间：
2002-07-25
影响因子：
3.9
通讯作者：
Franklin, SJ
中科院分区：
文献类型：
--
作者：
Sirish, M;Franklin, SJ
设计了一种嵌合肽(P4)，将EF-手金属结合环整合到增强同源结构域的螺旋-转弯-螺旋DNA结合基序中。这种结构结合了稀土元素，并在这些金属的存在下，促进了超螺旋DNA和模型磷酸酯(双硝基苯磷酸酯)的裂解。P4以中等亲和力键合稀土元素(Eu(III)，logK-a=4.85；Ce(IV)，logK-a=5.23)。金属结合增强了P4的结构，但CD观察到的二级结构增加不大，表明金属多肽也具有相当的柔韧性。尽管有这种灵活性，在低浓度下DNA的有效切割依赖于金属多肽，而不仅仅是多肽或金属。这种增强的反应活性表明，设计的与DNA结合的EF-手肽将金属输送到DNA进行催化，即使没有刚性的二级结构也是如此。(C)2002年，爱思唯尔科学公司出版。
A chimeric peptide (P4) has been designed to incorporate an EF-hand metal-binding loop into the context of the helix-turn-helix DNA binding motif of the engrailed homeodomain. This construct binds lanthanides, and in the presence of these metals, promotes the cleavage of supercoiled DNA and model phosphate esters (bisnitrophenyl phosphate). P4 binds lanthanides with moderate affinities (Eu(III), log K-a = 4.85; and Ce(IV), log K-a = 5.23). The structure of P4 is enhanced by metal binding, but the increase in secondary structure observed by CD is small, and suggests the metallopeptide is also quite flexible. Despite this flexibility, the efficient cleavage of DNA at low concentrations is dependent on the metallopeptide, and not on peptide or metal alone. This enhanced reactivity suggests the designed DNA-binding EF-hand peptides deliver the metal to the DNA for catalysis, even without rigid secondary structure. (C) 2002 Published by Elsevier Science Inc.