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- W2038973724 abstract "The antimicrobial peptide PMAP-36 exists as a homodimer stabilized by an intermolecular disulfide bridge. The dimer of PMAP-36 exhibits a potent and rapid microbicidal activity against a wide spectrum of microorganisms. The gene encoding the antiparallel dimer (PMAP-36)<sub>2</sub> was designed and codon-optimized according to bias of <i>Pichia pastoris</i>. The gene was then expressed in the <i>P. pastoris</i> strain GS115. The concentration of the recombinant product reached 106 mg/l. In vitro activity assays indicated that the recombinant peptide showed antimicrobial activities against Gram-positive and Gram-negative bacteria but did not cause hemolysis of chicken erythrocytes. Subsequently, 120 7-day-old male Arbor Acres broilers were used to evaluate the in vivo activities of the peptide. A prophylactic dose of ciprofloxacin lactate was supplemented as the control. The results showed that recombinant (PMAP-36)<sub>2</sub> significantly increased the serum IgM content of the birds (p < 0.05). The recombinant peptide significantly increased the amounts of <i>Bifidobacterium</i> and decreased the amount of <i>Escherichia coli</i> cells in the ceca of the experimental birds (p < 0.05). The results obtained in the present study indicate that the recombinant (PMAP-36)<sub>2</sub> has a potent in vitro and in vivo activity and can be used as an alternative to antibiotic treatment." @default.
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- W2038973724 date "2014-01-01" @default.
- W2038973724 modified "2023-10-18" @default.
- W2038973724 title "In vitro and in vivo Activity of the Dimer of PMAP-36 Expressed in <b><i>Pichia pastoris</i></b>" @default.
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- W2038973724 doi "https://doi.org/10.1159/000365572" @default.
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