Synthesis, characterization, and solution conformational analysis of C alpha-methyl-, C alpha-benzylglycine [(alpha Me)Phe] model peptides.
We have synthesized, by solution methods, and fully characterized a variety of (alpha Me)Phe derivatives and model peptides (to the pentapeptide level). The results of the solution conformational analysis, performed by using infrared absorption and 1H nuclear magnetic resonance, support the view that the (alpha Me)Phe residue is a stronger beta-turn and helix promoter than the unmethylated Phe analog. A comparison is also made with the conclusions extracted from published work on peptides rich in other C alpha-alkylglycyl residues.
Toniolo
C
C
Department of Organic Chemistry, University of Padova, Italy.
Formaggio
F
F
Crisma
M
M
Bonora
G M
GM
Pegoraro
S
S
Polinelli
S
S
Boesten
W H
WH
Schoemaker
H E
HE
Broxterman
Q B
QB
Kamphuis
J
J
D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry; D012996:Solutions / Q000737:chemistry; D013055:Spectrophotometry, Infrared
D009842:Oligopeptides; D012996:Solutions; C012436:alpha-methylphenylalanine; D010649:Phenylalanine