Biological and structural properties of cyclic peptides derived from the α-amylase inhibitor tendamistat

Bioscience, Biotechnology and Biochemistry

Volumn 62, Issue 8, 1998, Pages 1621-1623

  Ono, Shin ^a   Hirano, Tomiya ^a   Yasutake, Hiroki ^a,b   Matsumoto, Toshihiko ^a,b   Yamaura, Izumi ^a,b   Kato, Tetsuo ^a,b   Morita, Hiroyuki ^a   Fujii, Takayoshi ^a   Yamazaki, Isao ^a,c   Shimasaki, Choichiro ^a  

^a UNIVERSITY OF TOYAMA   (Japan)

^b SOJO UNIVERSITY   (Japan)

^c Yayoi Kagaku Kogyo Co Ltd   (Japan)

Author keywords

Circular dichroism; Cyclic peptides; Inhibitory activity; Porcine pancreatic amylase; Tendamistat

Indexed keywords

AMYLASE; CYCLOPEPTIDE; CYSTEINE; ENZYME INHIBITOR; PEPTIDE; TENDAMISTATE;

ANIMAL; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; DRUG ANTAGONISM; ENZYMOLOGY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KINETICS; MASS SPECTROMETRY; MOLECULAR GENETICS; PANCREAS; STRUCTURE ACTIVITY RELATION; SWINE; SYNTHESIS;

ALPHA-AMYLASE; ANIMALS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; CYSTEINE; ENZYME INHIBITORS; KINETICS; MOLECULAR SEQUENCE DATA; PANCREAS; PEPTIDES; PEPTIDES, CYCLIC; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STRUCTURE-ACTIVITY RELATIONSHIP; SWINE;

EID: 0032133314     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.62.1621     Document Type: Article

References (14)

1. Vértesy, L., Oeding, V., Bender, R., Zepf, K., and Nesemann, G., Tendamistat (HOE 467), a tight-binding a-amylase inhibitor from Streptomyces tendae 4158. Eur. J. Biochem., 141, 505-512 (1984).
2. Pflugrath, J. W., Wiegand, G., Huber, R., and Vértesy, L., Crystal structure determination, refinement and the molecular model of the a-amylase inhibitor Hoe-467A. J. Mol. Biol., 189, 383-386 (1986).
3. 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor tendamistat. J. Mol. Biol., 189, 377-382 (1986).
4. Qiwen, W., Kline, A. D., and Wüthrich, K., Amide proton exchange in the a-amylase polypeptide inhibitor tendamistat studied by two-dimensional *H nuclear magnetic resonance. Biochemistry, 26, 6488-6493 (1987).
5. Wiegand, G., Epp, O., and Huber, R., The crystal structure of porcine pancreatic a-amylase in complex with the microbial inhibitor tendamistat. J. Mol. Biol., 247, 99-110 (1995).
6. O’Connell, J. F., Bender, R., Engels, J. W., Roller, K.-P., Scharf, M., and Wüthrich, K., The nuclear-magnetic-resonance solution structure of the mutant a-amylase inhibitor [R19L]ten-damistat and comparison with wild-type tendamistat. Eur. J. Biochem., 220, 763-770 (1994).
7. Blanco, F. J., Jiménez, M. A., Rico, M., Santoro, J., Herranz, J., and Nieto, J. L., Tendamistat (12-26) fragment: NMR characterization of isolated β-turn folding intermediates. Eur. J. Biochem., 200, 345-351 (1991).
8. Blanco, F. J., Jiménez, M. A., Herranz, J., Rico, M., Santoro, J., and Nieto, J. L., NMR evidence of a short linear peptide that folds into a β-hairpin in aqueous solution. J. Am. Chem. Soc., 115, 5887-5888 (1993).
9. Etzkorn, F. A., Guo, T., Lipton, M. A., Goldberg, S. D., and Bartlett, P. A., Cyclic hexapeptides and chimeric peptides as mimics of tendamistat. J. Am. Chem. Soc., 116, 10412-10425 (1994).
10. Matter, H. and Kessler, H., Structures, dynamics, and biological activities of 15 cyclic hexapeptide analogs of the a-amylase inhibitor tendamistat (HOE 467) in solution. J. Am. Chem. Soc., 117, 3347-3359 (1995).
11. Tian Z.-Q. and Bartlett, P. A., Metal coordination as a method for templating peptide conformation. J. Am. Chem. Soc., 118, 943-949 (1996).
12. Sefler, A. M., Kozlowski, M. C., Guo, T., and Bartlett, P. A., Design, synthesis, and evaluation of a depsipeptide mimic of tendamistat. J. Org. Chem., 62, 93-102 (1997).
13. 4-0-β-d-galactopyranosyl-β-maltotetraoside). Clin. Chim. Acta, 234, 177-179 (1995).
14. Chou, P. Y. and Fasman, G. D., Prediction of protein conformation. Biochemistry, 13, 222-245 (1974).