Biological and structural properties of cyclic peptides derived from the alpha-amylase inhibitor tendamistat.
Six cyclic peptides with 5, 7, 9, 11, 13, and 15 amino acids, with the inhibitory sequence of the alpha-amylase inhibitor tendamistat, were synthesized. The 11-residue peptide inhibited porcine pancreatic alpha-amylase most potently (K1 0.29 +/- 0.09 microM). For the 11-residue peptide, the circular dichroism study suggested a preliminary relationship between its inhibitory activity and structural property.
Department of Chemical and Biochemical Engineering, Toyama University, Japan. shinono@eng.toyama-u.ac.jp
S
S
Ono
T
T
Hirano
H
H
Yasutake
T
T
Matsumoto
I
I
Yamaura
T
T
Kato
H
H
Morita
T
T
Fujii
I
I
Yamazaki
C
C
Shimasaki
T
T
Yoshimura
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D003545:Cysteine / Q000737:chemistry; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D007700:Kinetics; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013329:Structure-Activity Relationship; D013552:Swine; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
D004791:Enzyme Inhibitors; D010455:Peptides; D010456:Peptides, Cyclic; D000516:alpha-Amylases; D003545:Cysteine; C030526:tendamistate