Sequence analysis, multiple alignment, and secondary structure analysis of Hp1404 peptide.

<p>(A) cDNA and deduced amino acid sequences of Hp1404.The deduced amino acid residues are shown below the corresponding nucleotide sequences. The signal peptide residues are underlined. The mature peptide residues are shaded in gray.The potential cleavage site for prohormone convertase is marked in rectangle. The potential polyadenylation signal aataaa is double underlined. (B) Multiple alignment of Hp1404 with other antimicrobial peptides. Sim%, the percentage of sequence identity relative to Hp1404. The different color represents the different homology level. StCT1 and StCT2 from the scorpion <i>Scorpiops tibetanus</i>, CT1-NDBP-5.17 from the scorpion <i>Urodacus yaschenkoi</i>, IsCT from the scorpion <i>Opisthacanthus madagascariensis</i>, OcyC2 from the scorpion <i>Opisthacanthus cayaporum</i>, pantinin 1 from the scorpion <i>Pandinus imperator</i>. (C) Helical wheel diagram of Hp1404 determined by the Heliquest method. The representation of Hp1404 as a helical wheel shows the hydrophilic face and hydrophobic face. (D) CD spectra of Hp1404 peptide (100 µg/mL) in water alone or with 30 or 70% aqueous TFE.