An investigation of the conformation of peptide-T and its D-Ala analog by NMR and molecular dynamics simulations.
Indian J Biochem Biophys
;
1998 Jun; 35(3): 133-41
Article
in English
| IMSEAR
| ID: sea-26929
ABSTRACT
Peptide-T (ASTTTNYT) and its D-Ala analog (D-ASTTTNYT-NH2) have been designed to block the adsorption of HIV to CD4 receptors on T-cell lymphocytes, thus inhibiting viral infectivity. The conformation of these important peptides has been investigated by 2D-NMR and molecular dynamics simulations. The NMR studies in DMSO show that the peptides exist in solution as a mixture of conformations. beta-Turns and non-specific folded conformations are present in a small proportion in the ensemble of conformations, which is largely dominated by more or less extended structures. This result is in line with molecular dynamics simulations where beta-turns were found to occur with a low frequency and with energies 10 to 17 kcal/mole higher than the global minimum structure. Our findings differ from previous reports on the conformation of peptide-T determined by NMR.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Antiviral Agents
/
Magnetic Resonance Spectroscopy
/
Models, Molecular
/
Peptide T
/
HIV
/
Protein Structure, Secondary
/
Molecular Conformation
Type of study:
Prognostic study
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1998
Type:
Article
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