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Biological and structural properties of cyclic peptides derived from the alpha-amylase inhibitor tendamistat. 1998
S Ono, and
T Hirano, and
H Yasutake, and
T Matsumoto, and
I Yamaura, and
T Kato, and
H Morita, and
T Fujii, and
I Yamazaki, and
C Shimasaki, and
T Yoshimura
Department of Chemical and Biochemical Engineering, Toyama University, Japan. shinono@eng.toyama-u.ac.jp
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.
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