Abstract：
β-Hairpin peptides with RNA-binding sequences mimicking the central two β-strands of the RNA recognition motif (RRM) protein domain have been observed to bind in a 2:1 fashion to a series of RNA homooligonucleotides in aqueous solution (PBS buffer, pH 7.40) with binding energies (-27 to -35 kJ mol-1) similar to those of full-size protein RRMs. The peptides display mild selectivities with respect to the binding of the different homooligomers. Binding studies in 500 mM magnesium chloride suggest that the complex formation is not predominantly driven by Coulombic attraction. These peptides represent a starting point for further studies of non-Coulombic binding of RNA by peptides and proteins, which is important in the context of contemporary biology, potential therapeutic applications, and prebiotic peptide-RNA interactions.
摘要：
已观察到具有模拟RNA识别基序（RRM）蛋白结构域的中央两条β链的RNA结合序列的β发夹肽以2：1的方式与水溶液中的一系列RNA同源寡核苷酸结合（PBS缓冲液，pH7.40），其结合能（-27至-35kJmol-1）类似于全尺寸蛋白RRM的结合能。这些肽对不同均聚物的结合表现出温和的选择性。在500mM氯化镁中的结合研究表明,复合物形成并非主要由库仑吸引驱动。这些肽代表了进一步研究肽和蛋白质与RNA的非库仑结合的起点。这在当代生物学的背景下很重要，潜在的治疗应用，和益生元肽-RNA相互作用。
