Related Experiment Video
Updated: Jul 15, 2025

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
Published on: May 13, 2010
An Analysis of Nucleotide-Amyloid Interactions Reveals Selective Binding to Codon-Sized RNA
Saroj K Rout1, Riccardo Cadalbert1, Nina Schröder2
1Institute of Molecular Physical Science, ETH Zürich, 8093 Zürich, Switzerland.
Abstract:
Interactions between RNA and proteins are the cornerstone of many important biological processes from transcription and translation to gene regulation, yet little is known about the ancient origin of said interactions. We hypothesized that peptide amyloids played a role in the origin of life and that their repetitive structure lends itself to building interfaces with other polymers through avidity. Here, we report that short RNA with a minimum length of three nucleotides binds in a sequence-dependent manner to peptide amyloids. The 3'-5' linked RNA backbone appears to be well-suited to support these interactions, with the phosphodiester backbone and nucleobases both contributing to the affinity. Sequence-specific RNA-peptide interactions of the kind identified here may provide a path to understanding one of the great mysteries rooted in the origin of life: the origin of the genetic code.
Related Concept Videos
Nucleic Acid Structure
DNA Structure
DNA...
RNA Editing
Leaky Scanning
Nucleic Acids
DNA and RNA
The two main types of nucleic acids are deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). DNA is the genetic material in all living organisms, ranging from single-celled bacteria to multicellular mammals. It is in the nucleus of eukaryotes and in the organelles, chloroplasts, and mitochondria. In prokaryotes,...
RNA Stability
tRNA Activation

