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Retention of native-like structure in an acyclic counterpart of a beta-sheet antibiotic
R A Maplestone1, J P Cox, D H Williams
1Cambridge Centre for Molecular Recognition, University Chemical Laboratory, UK.
FEBS Letters
|July 12, 1993
Abstract:
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.