Generic placeholder image

Protein & Peptide Letters

Author(s): Deborah L. Heyl, Shakila Tobwala, Leo Solomon Lucas, A. Dammika Nandanie, Rebecca W. Himm, Jennifer Kappler, Elizabeth J. Blaney, Jason Groom, Jeffrey Asbill, Jonathan K. Nzoma, Cara Jarosz,, Hanna Palamma and Stephen E. Schullery

DOI: 10.2174/0929866053587110

DownloadDownload PDF Flyer Cite As
Peptide Inhibitors of a-Amylase Based on Tendamistat: Development of Analogues with ϖ-Amino Acids Linking Critical Binding Segments

Page: [275 - 280] Pages: 6

  • * (Excluding Mailing and Handling)

Explore Articles
About Journal
For Authors
For Editors
For Reviewers

Abstract

Peptide analogues of Tendamistat which include the most essential residues linked by novel w-amino acids (X,Y,Z: H2N-(CH2)n-CO2H, where n=2-10) were designed, synthesized (Ac-Tyr15-X-Trp18-Arg19-Tyr20-Y-Thr55-Z-Asp58- Gly59-Tyr60-Ile61-Gly62-NH2), and analyzed for α-amylase inhibitory activity. Native dipeptide spacers sometimes were left intact at X and Z. Analogues demonstrated competitive inhibition with Ki values ranging from 23 to 767 μM. 8- Aminooctanoic acid was the optimal linker at Y, while longer linkers were favored at the other positions.

Keywords: amylase, inhibitor, tendamistat, binding segment, linker