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Confirmation-dependent organic phosphor reveals amino acid nanoaggregates in ice with insight for prebiotic chemistry

Summary

Scientists have discovered that when amino acids (the building blocks of proteins) freeze in water ice, they naturally clump together into tiny particles called nanoaggregates. Using a special glowing molecule as a detector, researchers directly observed these clumps for the first time using electron microscopes. This finding suggests that icy environments in space or on early Earth could have naturally concentrated amino acids and created the right conditions for them to link together into proteins, potentially contributing to the origin of life.

Background

Freezing-induced enrichment of organic solutes in ice has been hypothesized to play a crucial role in prebiotic chemistry and the origins of life. However, direct experimental evidence for the aggregation of dilute, water-soluble amino acids in ice has remained elusive. Understanding this process is essential for explaining how primitive icy environments could have facilitated the formation of complex biomolecules.

Objective

This study aims to provide direct experimental evidence of amino acid nanoaggregation in water ice using a conformation-sensitive organic phosphor. The research seeks to elucidate the mechanisms driving amino acid aggregation and to demonstrate how these nanoaggregates could facilitate prebiotic peptide polymerization in early Earth conditions.

Results

Cryo-TEM images directly revealed uniform nanoaggregates of amino acids (leucine, isoleucine, glutamic acid, and others) in ice at nanometer scales (1-20 nm). Temperature-dependent Raman spectroscopy showed that amino acids undergo a proton-transfer transition from their ammonium to carboxylate groups at 180 K, increasing hydrophobicity and triggering aggregation. SNI exhibited amino-acid-specific conformation-dependent phosphorescence signatures reflecting the distinct surface morphologies of different amino acid aggregates.

Conclusion

This work provides direct evidence that amino acids form nanoaggregates in ice through a temperature-dependent proton-transfer process that enhances hydrophobicity. These nanoaggregates represent a critical first step in prebiotic peptide formation, preceding freeze-concentration and polymerization. The findings highlight ice as a significant medium for prebiotic molecular evolution and provide new insights into how primitive icy environments could have influenced the chemical origins of life.
  • Published in:Nature Communications,
  • Study Type:Experimental Research,
  • Source: 10.1038/s41467-025-65885-8, PMID: 41339311
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