Document Detail

Conformational analysis of dolastatin 10: an NMR and theoretical approach.
MedLine Citation:
PMID:  7578946     Owner:  NLM     Status:  MEDLINE    
A solution conformational analysis of dolastatin 10, a powerful antineoplastic agent, has been carried out by means of nmr techniques and theoretical calculations. 1H mono- and bidimensional nmr experiments, as well as 1H-13C heterocorrelated spectra, have been performed on CD2Cl2 solutions. The most interesting nmr data is a huge shielding of the aCH(25) proton of the Dov residue, suggesting the presence of an interaction between the N-terminal and the aromatic C-terminal ends of the molecule. The possibility of a head-to-tail intermolecular association having been discarded, the presence of a series of preferred folded conformation has been hypothesized. Conformational theoretical analysis supports the nmr hypothesis of a folded peptide-like molecule, and a series of possible conformers in good agreement with the experimental data have been analyzed.
E Benedetti; T Carlomagno; F Fraternali; Y Hamada; K Hayashi; L Paolillo; T Shioiri
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biopolymers     Volume:  36     ISSN:  0006-3525     ISO Abbreviation:  Biopolymers     Publication Date:  1995 Oct 
Date Detail:
Created Date:  1995-12-14     Completed Date:  1995-12-14     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0372525     Medline TA:  Biopolymers     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  525-38     Citation Subset:  IM    
Department of Chemistry, University of Naples, Italy.
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MeSH Terms
Amino Acid Sequence
Antineoplastic Agents / chemistry*
Magnetic Resonance Spectroscopy / methods
Models, Molecular*
Models, Theoretical
Molecular Sequence Data
Oligopeptides / chemistry*
Protein Conformation*
Protein Folding
Reg. No./Substance:
0/Antineoplastic Agents; 0/Depsipeptides; 0/Oligopeptides; 110417-88-4/dolastatin 10

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