Retention of native-like structure in an acyclic counterpart of a beta-sheet antibiotic.
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 beta-sheet characteristic of the intact ramoplanin persists. Thus, despite losing the entropic benefit which the macrocycle must lend to beta-sheet formation, the polypeptide chain of the acyclic ramoplanin appears to display an innate tendency to adopt a native-like conformation.
Maplestone
R A
RA
Cambridge Centre for Molecular Recognition, University Chemical Laboratory, UK.
Cox
J P
JP
Williams
D H
DH
D000900:Anti-Bacterial Agents / Q000737:chemistry*; D047630:Depsipeptides; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010456:Peptides, Cyclic; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012995:Solubility; D012996:Solutions
D000900:Anti-Bacterial Agents; D047630:Depsipeptides; D010456:Peptides, Cyclic; D012996:Solutions; C041438:ramoplanin