Comparison of the conformations of cyclolinopeptide A in the solid state and in solution.
Cyclolinopeptide A, a cyclic nonapeptide isolated from linseed, has lately attracted large interest for its cytoprotective activity. The recent elucidation of its solid state structure has prompted us to undertake a detailed conformational analysis in solution. Room-temperature 1H-nmr spectra in several solvents (DMSO-d6, DMSO-d6/D2O/H2O, CD3OH, (CD3)2CDOH, CDCl3) all show very broad lines, indicating the presence of chemical exchange among several conformers. It proved possible to freeze a single conformational state in CDCl3 at 214 K. Unusual chemical shifts and nuclear Overhauser enhancements are consistent with the main features of the solid state structure.
Tancredi
T
T
Zanotti
G
G
Rossi
F
F
Benedetti
E
E
Pedone
C
C
Temussi
P A
PA
D010456:Peptides, Cyclic / Q000138:chemical synthesis; D011487:Protein Conformation; D012996:Solutions
D010456:Peptides, Cyclic; D012996:Solutions; C055018:cyclolinopeptide A