Creating prebiotic sanctuary: self-assembling supramolecular Peptide structures bind and stabilize RNA

Area of Science:

• Biochemistry
• Astrobiology
• Origin of Life Research

Background:

• The origin of life requires a system that is both spontaneously formable and capable of Darwinian evolution.
• Short aromatic peptides self-assemble into stable structures with unique properties relevant to early life.
• Diphenylalanine supramolecular assemblies serve as a model for studying peptide-RNA interactions in prebiotic conditions.

Purpose of the Study:

• To explore molecular co-evolution mechanisms between self-assembling peptides and RNA fragments.
• To investigate the role of short self-assembling peptides in the origins of life.
• To model the prebiotic molecular evolution facilitated by peptide assemblies.

Main Methods:

• Demonstrated spontaneous formation of self-assembling peptides via the salt-induced peptide formation (SIPF) pathway under prebiotic conditions.
• Utilized diphenylalanine supramolecular assemblies as a model system to study peptide-RNA interactions.
• Investigated the sequence-dependent binding and stabilization of ribonucleotides by peptide assemblies.

Main Results:

• Self-assembling peptides were spontaneously formed under prebiotic conditions using the SIPF pathway.
• Peptide assemblies demonstrated sequence-dependent binding and stabilization of ribonucleotides, enhancing their relative fitness.
• Peptide assembly formation was dependent on monomer homochirality, mirroring the homochirality of extant life.

Conclusions:

• Short self-assembling peptides can bind and stabilize RNA fragments, contributing to prebiotic molecular evolution.
• The homochirality requirement for peptide self-assembly aligns with the homochirality observed in all living organisms.
• A model is proposed where self-assembling peptides play a crucial role in the origin of life by facilitating molecular co-evolution.