Structures of peptides from alpha-amino acids methylated at the alpha-carbon.
The structural preferences of peptides (and depsipeptides) from the achiral MeAib and Hib residues, and the chiral Iva, (alpha Me) Val, (alpha Me) Leu, and (alpha Me) Phe residues, as determined by conformational energy computations, x-ray diffraction analyses, and 1H-nmr and spectroscopic studies, are reviewed and compared with literature data on Aib-containing peptides. The results obtained indicate that helical structures are preferentially adopted by peptides rich in these alpha-amino acids methylated at the alpha-carbon. Intriguing experimental findings on the impact of the chirality of Iva, (alpha Me) Val, and (alpha Me) Phe residues on helix screw sense are illustrated.
Toniolo
C
C
Department of Organic Chemistry, University of Padova, Italy.
Crisma
M
M
Formaggio
F
F
Valle
G
G
Cavicchioni
G
G
Precigoux
G
G
Aubry
A
A
Kamphuis
J
J
D000595:Amino Acid Sequence; D000621:Aminoisobutyric Acids / Q000737:chemistry*; D006885:Hydroxybutyrates / Q000737:chemistry*; D008745:Methylation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013237:Stereoisomerism; D014633:Valine / Q000737:chemistry*; D014961:X-Ray Diffraction
D000621:Aminoisobutyric Acids; D006885:Hydroxybutyrates; D010455:Peptides; C100049:2-aminoisobutyric acid; C017911:2-(methylamino)isobutyric acid; C032737:isovaline; C008039:2-hydroxyisobutyric acid; D014633:Valine