SOLUTION CONFORMATION OF ENOPEPTIN-A, A DEPSIPEPTIDE ANTIBIOTIC, USING 2D-NMR AND RESTRAINED MOLECULAR-DYNAMICS STUDIES

Studies on the solution conformation of the cyclic depsipeptide antibi otic enopeptin A have been carried out using 2D NMR and molecular mode lling techniques. The proton resonances of the antibiotic in DMSO-d(6) have been assigned by the use of TOCSY and ROESY experiments. The int erproton distance information obtained from the ROESY experiments have been used as the basis for elucidating the probable structures in sol ution. The restrained molecular dynamics technique was applied to calc ulate the structures in solution, and six resultant structures with fe wer distance constraint violations were obtained that satisfy the expe rimental restraints very well. The conformation of the cyclic moiety o f the molecule is well defined whereas the aliphatic chain segment is disordered.