Three-dimensional structure of the ion-chanel forming peptide trichorzianin TA VII bound to sodium dodecyl sulfate micelles
✍ Scribed by Eric Condamine; Sylvie Rebuffat; Yann Prigent; Isabelle Ségalas; Bernard Bodo; Daniel Davoust
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1998
- Tongue
- English
- Weight
- 202 KB
- Volume
- 46
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
3 U 4 J 5 Q 6 U 7 U 8 U 9 S 10 L 11 U 12 P 13 V 14 U 15 I 16 Q 17 Q 18 Fol 19 , is a nonadecapeptide member of the peptaibol antibiotics biosynthesized by Trichoderma soil fungi, which is characterized by a high proportion of the a,a-dialkylated amino acids, a-aminoisobutyric acid (Aib, U) and isovaline (Iva, J), an acetylated N-terminus and a C-terminal phenylalaninol (Pheol, Fol). The main interest in such peptides stems from their ability to interact with phospholipid bilayers and form voltage-dependent transmembrane channels in planar lipid bilayers. In order to provide insights into the lipid-peptide interaction promoting the voltage gating, the conformational study of TA VII in the presence of perdeuterated sodium dodecyl sulfate (SDS-d25) micelles has been carried out. 1 H sequential assignments have been performed with the use of two-dimensional homo-and -heteronuclear nmr techniques including double quantum filtered correlated spectroscopy, homonuclear Hartmann-Hahn, nuclear Overhauser effect spectroscopy, 1 H-13 C heteronuclear single quantum correlation, and heteronuclear multiple bond correlation. Conformational parameters, such as 3 J NHCaH coupling constants, temperature coefficients of amide protons (Dd/DT NH ) and quantitative nuclear Overhauser enhancement data, lead to detailed structural information. Ninety-eight threedimensional structures consistent with the nmr data were generated from 231 interproton distances and six F dihedral angle restraints, using restrained molecular dynamics and energy minimization calculations. The average rms deviation between the 98 refined structures and