| Autor: |
Ono, Shin, Umezaki, Makiko, Tojo, Nagisa, Hashimoto, Shuko, Taniyama, Hiroko, Kaneko, Takako, Fujii, Takayoshi, Morita, Hiroyuki, Shimasaki, Choichiro, Yamazaki, Isao, Yoshimura, Toshiaki, Kato, Tetsuo |
| Předmět: |
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| Zdroj: |
Journal of Biochemistry; 2001, Vol. 129 Issue 5, p783-790, 8p |
| Abstrakt: |
Tendamistat is a strong inhibitory protein of porcine pancreatic a-amylase (PPA) with a Ki value of 0.2 nM. To develop potent a-amylase inhibitors, we synthesized six odd-length cyclic peptides (5–15 residues) and four even-length cyclic peptides (10 and 12 residues) having the inhibitory sequence of tendamistat. Their PPA inhibitory activities were evaluated, and, among them, the 11-residue cyclic peptide Ten(15–23)(Ki = 0.27–µM) exhibited the strongest inhibitory activity (Ki = 0.27–1.41 µM). To examine the effect of cyclic structure on PPA inhibition, ten linear peptides corresponding to the cyclic peptides were also synthesized, and their PPA inhibitory activities were evaluated (Ki = 0.28-1.00 µM). Interestingly, the 11-residue linear peptide Ten( 15–23) exhibited almost the same inhibitory activity (Ki = 0.28 µM) as that of cyclic Ten(15–23). The results of a circular dichroism study indicated that stabilization of the p-hairpin structure occurred only for cyclic Ten(15–23). Also, the results of proteolytic digestion experiments of the cyclic and linear Ten( 15–23) peptides by trypsin and chymotrypsin suggested no differences in protease resistance between the cyclic and linear structures. Therefore, we demonstrated that both cyclic and linear peptides containing the inhibitory sequence of tendamistat exhibit potent PPA inhibitory activity. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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