Abstract
Hybrid peptides (HP-MA, HP-ME), each of 20 residues and incorporating 2–9 residues of Helicobacter pylori ribosomal protein L1 (HP) and 1–12 residues of magainin 2 and melittin, were designed. The antibiotic activities of these peptides were evaluated using bacterial, tumor and human erythrocyte cells. HP-MA had a stronger antibacterial activity against Gram-positive bacteria and Gram-negative bacteria than HP (2-20) and magainin 2, and HP-ME was similar to melittin. None of the hybrids had anti-tumor or hemolytic activity. These peptides were further investigated using an artificial liposomal vesicle and 1,6-diphenyl-1,3,5-hexatriene as a membrane probe, and confirmed to have similar antibacterial activities. The antibacterial effect of these hybrids is probably caused by their ability to damage the bacterial plasma membrane. Additional circular dichroism spectra suggested that the α-helical structure of these peptides plays an important role in their antibiotic effect but that α-helical property is less connected with the enhanced antibiotic activity.
Similar content being viewed by others
References
Andreu D, Ubach J, Boman A, Wahlin D, Wade D, Merrifield RB, Boman HG (1992) Shortened cecropin A-melittin hybrids; significant size reduction retains potent antibiotic activity. FEBS Lett. 296: 190-194.
Binenbaum Z, Parola AH, Zaritzky A, Fishov I (1999) Transcription-and translation-dependent changes in membrane dynamics in bacteria: testing the transertion model for domain formation. Mol. Microbiol. 32: 1173-1182.
Boman HG, Wade D, Boman A, Wahlin B, Merrifield RB (1989) Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. FEBS Lett. 259: 103-106.
Chen H-C, Brown JH, Morell JL, Huang CM (1988) Synthetic magainin analogues with improved anti-microbial activity. FEBS Lett. 236: 462-466.
Lee DG, Shin SY, Kim D-H, Seo MY, Kang JH, Lee Y, Kim KL, Hahm K-S (1999) Antifungal mechanism of cysteine-rich antimicrobial peptide, Ib-AMP1, from Impatiens balsamina against Candida albicans. Biotechnol. Lett. 21: 1047-1050.
Lee DG, Shin SY, Maeng C-Y, Hahm K-S (1998) Cecropin Amelittin hybrid peptide exerts its antifungal effects by damaging on the plasma membranes of Trichosporon beigelii. Biotechnol. Lett. 20: 211-214.
MacDonald RC, MacDonald RI, Menco BP, Takeshita K, Subbarao NK, Hu L-R (1991) Small-volume extrusion apparatus for preparation of large, unilamellar vesicle. Biochim. Biophys. Acta 1061: 297-303.
Merrifield RB (1986) Solid phase synthesis. Science 232: 341-347.
Ohsaki Y, Gazdar AF, Chen HC, Johnson BE (1992) Antitumor activity of magainin analogues against human lung cancer cell lines. Cancer Res. 52: 3534-3538.
Pütsep K, Branden CI, Boman HG, Normark S (1999) Antibacterial peptide from H. pylori. Nature 398: 671-672.
Shin SY, Kang JH, Jang JS, Kim Y, Kim KL, Hahm K-S (2000) Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells. Biochim. Biophys. Acta 1463: 209-218.
Shin SY, Kang JH, LeeMK, Kim SY, Kim Y, Hahm K-S (1998) Cecropin A-magainin 2 hybrid peptides having potent antimicrobial activity with low hemolytic effect. Biochem. Mol. Biol. Intl. 44: 1119-1126.
Tosteson MT, Holmes SJ, Razin M, Tosteson DC (1985) Melittin lysis of red cells. J. Membr. Biol. 87: 35-44.
Zasloff M (1987) Magainins, a class of antimicrobial peptides from Xenopus skin: isolation characterization of two active forms, and partial cDNA sequence of precursor. Proc. Natl. Acad. Sci. USA 84: 5449-5453.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Keun Kim, H., Gun Lee, D., Park, Y. et al. Antibacterial activities of peptides designed as hybrids of antimicrobial peptides. Biotechnology Letters 24, 347–353 (2002). https://doi.org/10.1023/A:1014573005866
Issue Date:
DOI: https://doi.org/10.1023/A:1014573005866