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<p>Most of the peptides self-assembled into soft hydrogels in an aqueous environment, which disintegrated upon agitation. Two peptides, N-(9-Fluorenylmethyloxycarbonyl)-Anthranilic acid-L-Phenylalanine-L-Phenylalanine-L-Histidine amide (K) and N-(9-Fluorenylmethyloxycarbonyl)-Anthranilic acid-L-Phenylalanine-L-Histidine-L-Phenylalanine amide (L), formed stable hydrogels and exhibited storage moduli of 1.65 and 0.45&#xa0;kPa, respectively. Both peptides, K and L, effectively entrapped 5-Fluorouracil, with entrapment efficiencies of ~ 43% and ~ 58%, and drug loading efficiencies of ~ 21% and ~ 29%, respectively. Additionally, the cationic peptide, N-(9-Fluorenylmethyloxycarbonyl)-Anthranilic acid-L-Tyrosine-L-Phenylalanine-L-Arginine amide (J), formed a soft gel and exhibited antibacterial activity against <i>Klebsiella pneumoniae</i>, as evidenced by reduced colony-forming units (CFU). Likewise, the anionic peptide, N-(9-Fluorenylmethyloxycarbonyl)-L-Tryptophan-Anthranilic acid-L-Aspartic acid amide (D), showed antimicrobial activity against <i>Klebsiella pneumoniae</i> and <i>Staphylococcus aureus</i>, with minimum inhibitory concentrations of 100 and 200&#xa0;μg/mL, respectively. Peptides D, J, K, and L demonstrated cytocompatibility up to 400&#xa0;μg/mL in MCF-7 and HEK-293&#xa0;T cells. Overall, these results highlight the potential of these peptides as multifunctional biomaterials.</p> Graphical Abstract <p></p>

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Exploring tunable characteristics of anthranilic acid in peptide-based nanostructures

  • 期刊论文

  • 发表日期：

    2025年9月2日

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  • Nikita Verma,
  • Manohar Mahato,
  • Uma Dhawan,
  • Pradeep Kumar

摘要

Most of the peptides self-assembled into soft hydrogels in an aqueous environment, which disintegrated upon agitation. Two peptides, N-(9-Fluorenylmethyloxycarbonyl)-Anthranilic acid-L-Phenylalanine-L-Phenylalanine-L-Histidine amide (K) and N-(9-Fluorenylmethyloxycarbonyl)-Anthranilic acid-L-Phenylalanine-L-Histidine-L-Phenylalanine amide (L), formed stable hydrogels and exhibited storage moduli of 1.65 and 0.45 kPa, respectively. Both peptides, K and L, effectively entrapped 5-Fluorouracil, with entrapment efficiencies of ~ 43% and ~ 58%, and drug loading efficiencies of ~ 21% and ~ 29%, respectively. Additionally, the cationic peptide, N-(9-Fluorenylmethyloxycarbonyl)-Anthranilic acid-L-Tyrosine-L-Phenylalanine-L-Arginine amide (J), formed a soft gel and exhibited antibacterial activity against Klebsiella pneumoniae, as evidenced by reduced colony-forming units (CFU). Likewise, the anionic peptide, N-(9-Fluorenylmethyloxycarbonyl)-L-Tryptophan-Anthranilic acid-L-Aspartic acid amide (D), showed antimicrobial activity against Klebsiella pneumoniae and Staphylococcus aureus, with minimum inhibitory concentrations of 100 and 200 μg/mL, respectively. Peptides D, J, K, and L demonstrated cytocompatibility up to 400 μg/mL in MCF-7 and HEK-293 T cells. Overall, these results highlight the potential of these peptides as multifunctional biomaterials.

Graphical Abstract