Heterodimer Formation between the Antimicrobial Peptides Magainin 2 and PGLa in Lipid Bilayers: A Cross-Linking Study

The antimicrobial peptides magainin 2 and PGLa, isolated from the skin of the African clawed frog Xenopus laevis, show marked synergism [Westerhoff, H. V., Zasloff, M., Rosner, J. L., Hendler, R. W., de Waal, A., Vaz Gomes, A., Jongsma, A. P. M., Riethorst, A., and Juretić, D. (1995) Eur. J. Biochem...

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Published in:	Biochemistry (Easton) Vol. 40; no. 41; pp. 12395 - 12399
Main Authors:	Hara, Toshiaki, Mitani, Yasuyuki, Tanaka, Kyoko, Uematsu, Natsuko, Takakura, Asako, Tachi, Tomoya, Kodama, Hiroaki, Kondo, Michio, Mori, Harumi, Otaka, Akira, Nobutaka, Fujii, Matsuzaki, Katsumi
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 16-10-2001
Subjects:	Amino Acid Sequence Animals Antimicrobial Cationic Peptides - administration & dosage Antimicrobial Cationic Peptides - chemical synthesis Antimicrobial Cationic Peptides - chemistry Cross-Linking Reagents Dimerization Drug Design Drug Synergism In Vitro Techniques Lipid Bilayers Magainins Molecular Sequence Data Permeability Protein Precursors - administration & dosage Protein Precursors - chemical synthesis Protein Precursors - chemistry Xenopus laevis Xenopus Proteins
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Summary:	The antimicrobial peptides magainin 2 and PGLa, isolated from the skin of the African clawed frog Xenopus laevis, show marked synergism [Westerhoff, H. V., Zasloff, M., Rosner, J. L., Hendler, R. W., de Waal, A., Vaz Gomes, A., Jongsma, A. P. M., Riethorst, A., and Juretić, D. (1995) Eur. J. Biochem. 228, 257−264]. We suggested previously that these peptides form a potent heterodimer composed of either parallel or antiparallel helices in membranes [Matsuzaki, K., Mitani, Y., Akada, K., Murase, O., Yoneyama, S., Zasloff, M., and Miyajima, K. (1998) Biochemistry 37, 15144−15153]. To detect the putative heterodimer by chemical cross-linking, analogues of magainin 2 and PGLa with a Cys residue at either terminus were synthesized. These cross-linking experiments suggested that both peptides form a parallel heterodimer in membranes composed of phosphatidylglycerol/phosphatidylcholine but not in either buffer or a helix-promoting 2,2,2-trifluoroethanol/buffer mixture. The isolated parallel heterodimers exhibited an order of magnitude higher membrane permeabilization activity compared with the monomeric species, indicating that the observed synergism is due to heterodimer formation.
Bibliography:	ark:/67375/TPS-7Z53K404-6 istex:6E51DE3EA84DA8138F97BA15CBC341D1859C6F7B Supported in part by the Inamori Foundation, the Shimizu Foundation for the Promotion of Immunology Research, and Grant-in-Aid for Scientific Research for Advanced Area (A-13024244) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan. ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23
ISSN:	0006-2960 1520-4995
DOI:	10.1021/bi011413v