Literature DB >> 9757571

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

S Ono1, T Hirano, H Yasutake, T Matsumoto, I Yamaura, T Kato, H Morita, T Fujii, I Yamazaki, C Shimasaki, T Yoshimura.   

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.

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Year:  1998        PMID: 9757571     DOI: 10.1271/bbb.62.1621

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  1 in total

1.  Templating α-amylase peptide inhibitors with organotin compounds.

Authors:  Fernando Porcelli; Cristina Olivieri; Larry R Masterson; Yi Wang; Gianluigi Veglia
Journal:  J Biol Inorg Chem       Date:  2011-07-07       Impact factor: 3.358

  1 in total

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