Cysteine-Based Dynamic Self-Assembly and Their Importance in the Origins of Life

The knowledge regarding the origins of life from inanimate materials is still elusive. It was proposed that biological building blocks evolved from the inorganic substances present in the early earth conditions. However, the process by which chemistry can be converted into biology has not yet been achieved in the laboratory. The artificial system in the out-of-equilibrium state must maintain a few critical features of life, like compartmentalization, metabolism, and replication, to be considered alive. In this direction, working with cysteine (Cys)-based molecules is strategic to understand the life evolution process. The presence of the sulphydryl (-SH) group in the Cys-residue can build a dynamic equilibrium state through disulfide redox chemistry under the proper guidance of oxidizing and reducing agents. In this review article, our primary focus is to discuss the Cys-containing short-peptide-based self-assembly and disassembly processes. The formation of disulfide bonds sometimes helps in the self-assembly process and gelation, but the reverse is also true in some cases. In the later part of this article, we cover the fact that these sulphydryl-based systems have shown their adaptability to mimic different life-essential criteria to participate in Darwinian evolution. Cysteine-conjugated short-peptide-based dynamic self-assembly is one of the most important areas of research in understanding the emergence of life from inanimate substances. The redox-active nature of the disulfide bond provides dynamic control over the supramolecular assembly. Cysteine-based systems showed their potency in self-replication, compartmentalization, and metabolism processes to mimic life's essential criteria. image