Piscidin-3 exhibits a strongly amphipathic structure enabling membrane-interaction and α-helical formation. Charged residues support biophysical analyses of peptide–lipid interfaces. Folding transitions help model target specificity. The sequence is widely used in aquatic peptide research and structure–activity investigations.
CAT No: P26009
2. Implications of ligand-receptor binding kinetics on GLP-1R signalling
5. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
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