Like RGG domains in FUS proteins and LAF-1, repetitively charged homopeptides like polylysine (poly-K), poly-glutamate (poly-E), and poly-arginine (poly-R) are all unstructured, have low complexity, and contribute IDP phase separation. Some of these homopeptides can form phase-separated systems with RNA or with each other in vitro and therefore, have been associated with the formation of coacervates on primitive Earth. For example, poly-K-ATP coacervates can encapsulate primitive biochemical reactions and biomolecules while reversibly assembling and disassembling. pH and temperaturemediated reversible compartmentalization of poly-K-ATP coacervates inside of liposomes represents a membrane-bound protocell model containing functional coacervates, while poly-K and DNA liquid crystal coacervates have been hypothesized to aid in the evolution of prebiotic peptides and nucleic acids through multiple structural and functional complexity increasing prebiotic pathways. Poly-R has also been shown to form coacervates upon binding with nucleotides in vitro. poly-R-containing coacervates are more viscous than poly-K-containing coacervates, leading to the formation of a multiphase coacervate with a polyR core and a polyK shell. Formation of such multi-phase systems using simple homopeptides hint towards a possibility that such peptides could have paved the way towards the formation of coacervates of increasing complexity, thus bridging the gap between primitive and modern phase separation. Moreover, arginine is hypothesized to have formed even before lysine and could be considered to be the first canonical basic AA that originated on early Earth. Other than poly-K homopeptides, anionic homopeptides such as poly-aspartate (poly-D) and poly-E have also been used to produce prebiotically relevant coacervates in vitro. Thus, the ability of charged disordered homopeptides to form in vitro coacervates strengthens the hypothesis that primitive disordered peptides could have given rise to primitive coacervates on prebiotic Earth. However, rather than K, E, and R, G and alanine (A) homopeptides have been assumed