Prebiotic Peptide Synthesis: How Did Longest Peptide Appear?

Abstract

The origin of proteins is a fundamental question in the study of the origin of life. Peptides, as the building blocks of proteins, necessarily preceded the first proteins in prebiotic chemical evolution. Prebiotic peptides may have also played crucial roles in early life's evolution, contributing to self-catalysis, interacting with nucleic acids, and stabilizing primitive cell compartments. Longer and more complicated prebiotic peptides often have greater structural flexibility and functional potential to support the emergence and evolution of early life. Since the Miller-Urey experiment demonstrated that amino acids can be synthesized in a prebiotic manner, the prebiotic synthesis route of peptides has garnered increasing attention from researchers. However, it is difficult for amino acids to condense into peptides in aqueous solutions spontaneously. Over the past few decades, researchers have explored various routes of prebiotic peptide synthesis in the plausible prebiotic Earth environment, such as thermal polymerization, clay mineral catalysis, wet-dry cycles, condensing agents, and lipid-mediated. This paper reviews advancements in prebiotic peptide synthesis research and discusses the conditions that may have facilitated the emergence of longer peptides.