ArticleProtein and peptide letters2026
Design and TAG-Assisted Synthesis of the C-Terminal Amidated Antimicrobial Peptide NCBP-1 Derived from a Plant-Derived Noncanonical NCBP and Its Biological Activity.
Article in Protein and peptide letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
introductionThe rise in global bacterial resistance necessitates the discovery of novel antibiotics. Plant-derived Antimicrobial Peptides (AMPs) offer structural diversity and biocompatibility. This study aims to investigate the green synthesis and biological activities of derivatives of NCBP, a linear non-classical AMP identified from plants.
methodsFive NCBP derivatives (NCBP-1 to NCBP-5) were generated using a green tag-assisted peptide synthesis (TAPS) strategy, combined with site-directed mutagenesis and terminal modification. The peptides were characterized by MS and HPLC and subsequently evaluated for antibacterial activity against ten bacterial strains, salt tolerance, and cytotoxicity in RAW 264.7 murine macrophages. Molecular docking was performed to assess binding interactions.
resultsNCBP-1 was identified as the lead derivative, demonstrating potent antibacterial activity (MIC 8 μg·mL-¹) and low cytotoxicity. It also exhibited moderate anti-inflammatory activity in LPSstimulated RAW 264.7 macrophages. Its antibacterial mechanism was further supported by favorable molecular docking interactions with E. coli outer membrane LPS (PDB ID: 4RHB). DISCUSSION: The combined approach successfully identified NCBP-1 as a potent antibacterial candidate. Its activity against Gram-negative bacteria is likely related to LPS binding, as suggested by the docking results. Further studies would be needed to fully elucidate its mechanism of action.
conclusionNCBP-1 represents a promising lead for the development of novel antibacterial agents, particularly for treating Gram-negative bacterial infections.
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