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Biological and structural properties of cyclic peptides derived from the alpha-amylase inhibitor tendamistat
1Department of Chemical and Biochemical Engineering, Toyama University, Japan. shinono@eng.toyama-u.ac.jp
Bioscience, Biotechnology, and Biochemistry
|October 3, 1998
Abstract:
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.