Download MendeleyEvidence for Phenylalanine Zipper-Mediated Dimerization in the X-ray Crystal Structure of a Magainin 2 Analogue.
Hayouka, Z., Mortenson, D.E., Kreitler, D.F., Weisblum, B., Forest, K.T., Gellman, S.H.(2013) J Am Chem Soc 135: 15738-15741
- PubMed: 24102563
- DOI: https://doi.org/10.1021/ja409082w
- Primary Citation of Related Structures:
4MGP - PubMed Abstract:
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.
Organizational Affiliation:
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
