Mesh ： Amino Acid Sequence Amino Acid Substitution Animals Annelida / metabolism Anti-Infective Agents / chemical synthesis chemistry pharmacology Biological Transport / drug effects Cell Membrane Permeability / drug effects Circular Dichroism Consensus Sequence Conserved Sequence Dextrans / pharmacokinetics Fluorescein-5-isothiocyanate / analogs & derivatives pharmacokinetics Fungi / drug effects metabolism Gram-Negative Bacteria / drug effects Gram-Positive Bacteria / drug effects Hydrophobic and Hydrophilic Interactions Indicators and Reagents / pharmacokinetics Neuropeptides / chemistry Peptide Fragments / chemical synthesis chemistry pharmacology Propidium / pharmacokinetics Protein Structure, Secondary Tachykinins / chemistry

来  源：   DOI：10.1248/bpb.34.921   PDF(Sci-hub)

Abstract：
In our previous study, we reported that urechistachykinin I (U I) and II (U II) exerted antimicrobial effects. To find out how the tachykinin consensus sequence of the urechistachykinin peptide family affects its antimicrobial activity, analogues substituting the amino acid residues phenylalanine (Phe-6; Anal 1), glycine (Gly-8; Anal 2), and arginine (Arg-10; Anal 3) of U II to alanine (Ala) were designed. Subsequently, the antimicrobial activity was shown on the order of Anal 3>U II=Anal 2>Anal 1, and this activity pattern was correlated with membrane studies such as propidium iodide (PI) influx and fluorescein isothiocyanate dextran (FD) leakage assay. These results suggest that the antimicrobial activity is related to the hydrophobicity values of the peptides. In regards to the activity of U II, it is determined that the hydrophobic Phe-6 plays a more critical role than Gly-8 or Arg-10.
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