Peptides at vesicle and mineral prebiotic interfaces

The origin of life likely involved a complex interplay between organic molecules and mineral surfaces, yet the molecular details of these interactions remain poorly understood. Over recent decades, considerable research has focused on the individual roles of key biomolecules—such as RNA, lipids, and proteins—in early biogenesis. However, this reductionist view offers only a partial picture; the emergence of life likely involved networks of molecular interactions that collectively shaped early functional assemblies.

In this study, we examine the potential of peptides—arguably the most abundant early polymers— to interact with mineral surfaces and lipid vesicles, representing prebiotically plausible interfaces and compartments. Focusing on peptide compositions derived from prebiotically plausible amino acids, we demonstrate that such early peptides could bind mineral surfaces ( e.g. , fluorapatite) via negatively charged residues. Nevertheless, the recruitment of amino acids from the modern alphabet was likely adaptive for favorable interactions with lipid vesicles and could lead to enhanced functional behavior, such as promoting phosphate release. Our findings suggest that the evolving complexity of the peptide/protein alphabet was a key factor in the evolution of protocells and could enhance early catalytic functions at the interface of geochemistry and biochemistry.