Anti-peptide aptamers recognize amino acid sequence and bind a protein epitope

被引:116
作者
Xu, W [1 ]
Ellington, AD [1 ]
机构
[1] INDIANA UNIV,DEPT CHEM,BLOOMINGTON,IN 47405
关键词
in vitro selection; SELEX; combining site;
D O I
10.1073/pnas.93.15.7475
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
In vitro selection of nucleic acid binding species (aptamers) is superficially similar to the immune response, Both processes produce biopolymers that can recognize targets with high affinity and specificity. While antibodies are known to recognize the sequence and conformation of protein surface features (epitopes), very little is known about the precise interactions between aptamers and their epitopes, Therefore, aptamers that could recognize a particular epitope, a peptide fragment of human immunodeficiency virus type 1 Rev, were selected from a random sequence RNA pool. Several of the selected RNAs could bind the free peptide more tightly than a natural RNA ligand, the Rev-binding element. In accord with the hypothesis that protein and nucleic acid binding cusps are functionally similar, interactions between aptamers and the peptide target could be disrupted by sequence substitutions, Moreover, the aptamers appeared to be able to bind peptides with different solution conformations, implying an induced fit mechanism for binding, Just as anti-peptide antibodies can sometimes recognize the corresponding epitope when presented in a protein, the anti-peptide aptamers were found to specifically bind to Rev.
引用
收藏
页码:7475 / 7480
页数:6
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