This study investigates how RNA binding proteins, specifically hnRNPA1A, modulate the formation of amyloid fibrils through biomolecular condensates. hnRNPA1A, a protein involved in amyotrophic lateral sclerosis (ALS), forms dynamic condensates that eventually aggregate into amyloid fibrils. The presence of RNA, particularly at intermediate concentrations, promotes both condensation and amyloid formation, while higher RNA concentrations suppress condensation but do not prevent amyloid formation over longer incubation times. The study demonstrates that RNA can modulate the kinetics and molecular pathways of amyloid formation in a concentration-dependent manner, highlighting the complex interplay between RNA and protein interactions in the development of pathological amyloids. The findings contribute to our understanding of how heterotypic interactions between RNA and proteins affect the formation of amyloid fibrils in membraneless organelles.This study investigates how RNA binding proteins, specifically hnRNPA1A, modulate the formation of amyloid fibrils through biomolecular condensates. hnRNPA1A, a protein involved in amyotrophic lateral sclerosis (ALS), forms dynamic condensates that eventually aggregate into amyloid fibrils. The presence of RNA, particularly at intermediate concentrations, promotes both condensation and amyloid formation, while higher RNA concentrations suppress condensation but do not prevent amyloid formation over longer incubation times. The study demonstrates that RNA can modulate the kinetics and molecular pathways of amyloid formation in a concentration-dependent manner, highlighting the complex interplay between RNA and protein interactions in the development of pathological amyloids. The findings contribute to our understanding of how heterotypic interactions between RNA and proteins affect the formation of amyloid fibrils in membraneless organelles.