Identification and functional optimization of a novel pteroicidin-like peptide from starry flounder: Structure-activity insights into truncation and tryptophan substitution.
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| Natura: | Artículo científico |
| Lingua: | en |
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Fish & shellfish immunology
2026
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| _version_ | 1868266051097067522 |
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| author | Jeon, Yu-Jeong Lim, Han Kyu Choi, Mi-Jin |
| author_facet | Jeon, Yu-Jeong Lim, Han Kyu Choi, Mi-Jin Jeon, Yu-Jeong Lim, Han Kyu Choi, Mi-Jin |
| collection | PubMed - marine biology |
| contents | Identification and functional optimization of a novel pteroicidin-like peptide from starry flounder: Structure-activity insights into truncation and tryptophan substitution. Jeon, Yu-Jeong Lim, Han Kyu Choi, Mi-Jin Animals Fish Proteins Amino Acid Sequence Vibrio Fish Diseases Antimicrobial Cationic Peptides Sequence Alignment Structure-Activity Relationship Streptococcus Streptococcal Infections Vibrio Infections Immunity, Innate Gene Expression Regulation Antimicrobial Peptides Flounder Flatfishes Gene Expression Profiling Tryptophan Phylogeny Base Sequence Antimicrobial peptides of the piscidin family are key effectors of teleost innate immunity and represent promising alternatives to conventional antibiotics in aquaculture. Therefore, this study aimed to identify and characterize a novel pteroicidin-like gene (SFpte) from starry flounder (Platichthys stellatus). The deduced 64-amino-acid precursor comprised a signal peptide, 20-residue cationic α-helical mature peptide (SFpte-20; FFRHLKAIFKGARQGWRDYR), and C-terminal anionic propeptide. SFpte was constitutively expressed across tissues and significantly upregulated in the kidney and spleen following challenge with Vibrio harveyi and Streptococcus parauberis. To assess the structure-activity relationships, truncated (17-mer and 13-mer) analogs and tryptophan (Trp)-substituted variants were engineered. In silico modeling showed that truncation and Trp substitution modulated amphipathicity and membrane-transfer energetics, with H4W displaying favorable predicted membrane association (ΔG = -11.1 kcal/mol). All peptides exhibited broad-spectrum antimicrobial activity (minimum inhibitory concentration 2.5-10 μM), while selected Trp variants showed enhanced antimicrobial efficiency. The scanning electron microscope confirmed bacterial membrane disruption as the primary mode of action. All analogs rapidly killed the scuticociliate Philasterides dicentrarchi. Hemolysis was concentration-dependent; specifically, the truncated 13-mer retained antimicrobial potency while inducing minimal erythrocyte lysis ( |
| format | Artículo científico |
| id | pubmed_42107612 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Fish & shellfish immunology |
| record_format | pubmed |
| spellingShingle | Identification and functional optimization of a novel pteroicidin-like peptide from starry flounder: Structure-activity insights into truncation and tryptophan substitution. Jeon, Yu-Jeong Lim, Han Kyu Choi, Mi-Jin Animals Fish Proteins Amino Acid Sequence Vibrio Fish Diseases Antimicrobial Cationic Peptides Sequence Alignment Structure-Activity Relationship Streptococcus Streptococcal Infections Vibrio Infections Immunity, Innate Gene Expression Regulation Antimicrobial Peptides Flounder Flatfishes Gene Expression Profiling Tryptophan Phylogeny Base Sequence Identification and functional optimization of a novel pteroicidin-like peptide from starry flounder: Structure-activity insights into truncation and tryptophan substitution. Jeon, Yu-Jeong Lim, Han Kyu Choi, Mi-Jin Animals Fish Proteins Amino Acid Sequence Vibrio Fish Diseases Antimicrobial Cationic Peptides Sequence Alignment Structure-Activity Relationship Streptococcus Streptococcal Infections Vibrio Infections Immunity, Innate Gene Expression Regulation Antimicrobial Peptides Flounder Flatfishes Gene Expression Profiling Tryptophan Phylogeny Base Sequence Antimicrobial peptides of the piscidin family are key effectors of teleost innate immunity and represent promising alternatives to conventional antibiotics in aquaculture. Therefore, this study aimed to identify and characterize a novel pteroicidin-like gene (SFpte) from starry flounder (Platichthys stellatus). The deduced 64-amino-acid precursor comprised a signal peptide, 20-residue cationic α-helical mature peptide (SFpte-20; FFRHLKAIFKGARQGWRDYR), and C-terminal anionic propeptide. SFpte was constitutively expressed across tissues and significantly upregulated in the kidney and spleen following challenge with Vibrio harveyi and Streptococcus parauberis. To assess the structure-activity relationships, truncated (17-mer and 13-mer) analogs and tryptophan (Trp)-substituted variants were engineered. In silico modeling showed that truncation and Trp substitution modulated amphipathicity and membrane-transfer energetics, with H4W displaying favorable predicted membrane association (ΔG = -11.1 kcal/mol). All peptides exhibited broad-spectrum antimicrobial activity (minimum inhibitory concentration 2.5-10 μM), while selected Trp variants showed enhanced antimicrobial efficiency. The scanning electron microscope confirmed bacterial membrane disruption as the primary mode of action. All analogs rapidly killed the scuticociliate Philasterides dicentrarchi. Hemolysis was concentration-dependent; specifically, the truncated 13-mer retained antimicrobial potency while inducing minimal erythrocyte lysis ( |
| title | Identification and functional optimization of a novel pteroicidin-like peptide from starry flounder: Structure-activity insights into truncation and tryptophan substitution. |
| topic | Animals Fish Proteins Amino Acid Sequence Vibrio Fish Diseases Antimicrobial Cationic Peptides Sequence Alignment Structure-Activity Relationship Streptococcus Streptococcal Infections Vibrio Infections Immunity, Innate Gene Expression Regulation Antimicrobial Peptides Flounder Flatfishes Gene Expression Profiling Tryptophan Phylogeny Base Sequence |
| url | https://pubmed.ncbi.nlm.nih.gov/42107612/ |