NMR structure of the channel‐former zervamicin IIB in isotropic solvents

FEBS Letters

Arseniev, A.S.¹  Raap, J.²  Balashova, T.A.¹  Ovchinnikova, T.V.¹  Shenkarev, Z.O.¹  Tagaev, A.A.¹ 

[1] Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, 117871 Moscow, Russia;Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, Einsteinweg 55, P.O. Box 9502, 2300 RA Leiden, The Netherlands

关键词: Nuclear magnetic resonance;    Antibiotic;    Zervamicin;    Channel-former;    Peptaibol;    NMR;    nuclear magnetic resonance;    2D;    two-dimensional;    NOE;    nuclear Overhauser effect;    DQF-COSY;    2D double quantum filtered correlated spectroscopy;    NOESY;    2D NOE-correlated spectroscopy;    rmsd;    root mean square deviation;    TOCSY;    2D total correlated spectroscopy;    Zrv-IIB;    zervamicin IIB;   

DOI  :  10.1016/S0014-5793(99)01707-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Spatial structure of the membrane channel-forming hexadecapeptide, zervamicin IIB, was studied by NMR spectroscopy in mixed solvents of different polarity ranging from CDCl₃/CD₃OH (9:1, v/v) to CD₃OH/H₂O (1:1, v/v). The results show that in all solvents used the peptide has a very similar structure that is a bent amphiphilic helix with a mean backbone root mean square deviation (rmsd) value of ca. 0.3 Å. Side chains of Trp¹, Ile², Gln³, Ile⁵ and Thr⁶ are mobile. The results are discussed in relation to the validity of the obtained structure to serve as a building block of zervamicin IIB ion channels.

【 授权许可】

Unknown