Design of Amphiphilic Protein Maquettes: Controlling Assembly, Membrane Insertion, and Cofactor Interactions†
作者： Bohdana M. Discher , Dror Noy , Joseph Strzalka , Shixin Ye , Christopher C. Moser
DOI: 10.1021/BI050695M
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摘要: We have designed polypeptides combining selected lipophilic (LP) and hydrophilic (HP) sequences that assemble into amphiphilic (AP) α-helical bundles to reproduce key structure characteristics functional elements of natural membrane proteins. The principal AP maquette (AP1) developed here joins 14 residues a heme binding sequence from structured diheme-four-α-helical bundle (HP1), with 24 membrane-spanning LP domain the four-α-helical M2 channel influenza virus, through flexible linking (GGNG) make 42 amino acid peptide. individual AP1 helices (without connecting loops) in detergent as observed by analytical ultracentrifugation. are oriented parallel indicated interactions typical adjacent hemes. orients vectorially at nonpolar−polar interfaces readily incorporates phospholipid vesicles >97% efficiency, although most probably without vectorial bias. Mono- diheme−AP...
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