Gelinas Amy D, Davies Douglas R, Janjic Nebojsa
SomaLogic, Inc., 2945 Wilderness Place, Boulder, CO 80301, United States.
Beryllium, 7869 NE Day Road West, Bainbridge Island, WA 98110, United States.
Curr Opin Struct Biol. 2016 Feb;36:122-32. doi: 10.1016/j.sbi.2016.01.009. Epub 2016 Feb 24.
Understanding the structural rules that govern specific, high-affinity binding characteristic of aptamer-protein interactions is important in view of the increasing use of aptamers across many applications. From the modest number of 16 aptamer-protein structures currently available, trends are emerging. The flexible phosphodiester backbone allows folding into precise three-dimensional structures using known nucleic acid motifs as scaffolds that orient specific functional groups for target recognition. Still, completely novel motifs essential for structure and function are found in modified aptamers with diversity-enhancing side chains. Aptamers and antibodies, two classes of macromolecules used as affinity reagents with entirely different backbones and composition, recognize protein epitopes of similar size and with comparably high shape complementarity.
鉴于适配体在众多应用中的使用日益增加，了解支配适配体与蛋白质相互作用的特定、高亲和力结合特性的结构规则非常重要。从目前可用的数量不多的16种适配体 - 蛋白质结构中，趋势正在显现。灵活的磷酸二酯主链允许利用已知的核酸基序作为支架折叠成精确的三维结构，这些支架将特定的官能团定向用于靶标识别。尽管如此，在具有增强多样性侧链的修饰适配体中发现了对结构和功能至关重要的全新基序。适配体和抗体是两类用作亲和试剂的大分子，它们具有完全不同的主链和组成，识别大小相似且具有相当高形状互补性的蛋白质表位。
