In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.

In this study, we would investigate the co-modification of fatty acids and monosaccharides in anticancer peptides, as we expect to optimize the selectivity and cytotoxicity of the peptide at the same time. Based on our previous study, the lipopeptide R-C12 was selected as a template to perform glucose derivative modification at different positions as we supposed that the glucose derivative modification position in R-C12 might be a crucial factor in its selectivity and activity optimization. The glucose derivative was covalently coupled to different sites in R-C12 through its -amino group of a Lys residue, which was obtained by replacing the Arg residue. R-C12 contains seven Arg residues, accordingly, seven glycolipid peptides were designed and synthesized, which were named R-C12-1, R-C12-2, R-C12-3, R-C12-4, R-C12-5, R-C12-6, and R-C12-7. Various physiochemical properties including the hydrodynamic size, ζ-potential, secondary structure, and hydrophobicity were determined to explain the different cytotoxicity and selectivity of these glycolipid peptides. On the other hand, the strength of the binding between glycolipid peptides and the cancer cells mediated by GLUT1 has also been explored. The most optimized glycolipid peptide R-C12-4 demonstrated significant cytotoxicity and antimetastasis in vitro and in vivo, which indicated that it may be a good lead for anticancer drug development.