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XB-ART-49889
J Am Chem Soc 2013 Oct 23;13542:15738-15741. doi: 10.1021/ja409082w.
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Evidence for phenylalanine zipper-mediated dimerization in the X-ray crystal structure of a magainin 2 analogue.

Hayouka Z , Mortenson DE , Kreitler DF , Weisblum B , Forest KT , Gellman SH .


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High-resolution structure elucidation has been challenging for the large group of host-defense peptides that form helices on or within membranes but do not manifest a strong folding propensity in aqueous solution. Here we report the crystal structure of an analogue of the widely studied host-defense peptide magainin 2. Magainin 2 (S8A, G13A, G18A) is a designed variant that displays enhanced antibacterial activity relative to the natural peptide. The crystal structure of magainin 2 (S8A, G13A, G18A), obtained for the racemic form, features a dimerization mode that has previously been proposed to play a role in the antibacterial activity of magainin 2 and related peptides.

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Species referenced: Xenopus
Genes referenced: magainins

References [+] :
Ahmad, Design of nontoxic analogues of cathelicidin-derived bovine antimicrobial peptide BMAP-27: the role of leucine as well as phenylalanine zipper sequences in determining its toxicity. 2009, Pubmed