Retention of native‐like structure in an acyclic counterpart of a β‐sheet antibiotic

FEBS Letters

Williams, Dudley H.¹  Maplestone, Rachael A.¹  Cox, Jonathan P.L.¹ 

[1]Cambridge Centre for Molecular Recognition, University Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW UK

关键词: Loop formation;    Ramoplanin;    β-Sheet;    NMR;    2D;    Native-like conformation;    NOESY;    nuclear Overhauser enhancement spectroscopy;    TOCSY;    total correlated spectroscopy;    COSY;    1H-1H correlated spectroscopy;    DIPSI;    decoupling in the presence of scalar interactions;    NOE;    nuclear Overhauser enhancement;    TFA;    trifluoroacetic acid;    HPLC;    high-performance liquid chromatography;    UHP;    ultrahigh purity;    CHP;    (3-chloro-4-hydroxyphenyl)glycine;    HPG;    (4-hydroxyphenyl)glycine;    Orn;    ornithine;    (βOH)Asn;    (d-β-hydroxy)-l-as-paragine;   

DOI  :  10.1016/0014-5793(93)81769-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An acyclic derivative of the cyclic peptide antibiotic, ramoplanin, has been prepared. In aqueous solution, two-dimensional NMR spectroscopy indicates that the acyclic form adopts a threshold population of conformers in which at least part of the β-sheet characteristic of the intact ramoplanin persists. Thus, despite losing the entropic benefit which the macrocycle must lend to β-sheet formation, the polypeptide chain of the acyclic ramoplanin appears to display an innate tendency to adopt a native-like conformation.

【 授权许可】

Unknown