The article explores the potential of arginine-rich peptides as carriers for intracellular protein delivery. The study found that various arginine-rich peptides, including those derived from HIV-1 Tat protein, RNA-binding peptides, and DNA-binding segments, exhibit translocation activity similar to HIV-1 Tat-(48–60). These peptides can efficiently cross cell membranes and accumulate in the nucleus, even at low temperatures. The internalization mechanism of these peptides is distinct from typical endocytosis, suggesting the existence of a unique, undefined process. The optimal number of arginine residues (n = 8) was identified for efficient translocation. The peptides were also used to deliver carbonic anhydrase into cells, demonstrating their potential as carriers for therapeutic and research applications. The findings highlight the importance of arginine residues in the internalization process and suggest that arginine-rich peptides could be developed as novel carriers for intracellular protein delivery.The article explores the potential of arginine-rich peptides as carriers for intracellular protein delivery. The study found that various arginine-rich peptides, including those derived from HIV-1 Tat protein, RNA-binding peptides, and DNA-binding segments, exhibit translocation activity similar to HIV-1 Tat-(48–60). These peptides can efficiently cross cell membranes and accumulate in the nucleus, even at low temperatures. The internalization mechanism of these peptides is distinct from typical endocytosis, suggesting the existence of a unique, undefined process. The optimal number of arginine residues (n = 8) was identified for efficient translocation. The peptides were also used to deliver carbonic anhydrase into cells, demonstrating their potential as carriers for therapeutic and research applications. The findings highlight the importance of arginine residues in the internalization process and suggest that arginine-rich peptides could be developed as novel carriers for intracellular protein delivery.