Peptide inhibitors of α-amylase based on tendamistat: Development of analogues with ω-amino acids linking critical binding segments

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, Stephen E. Schullery

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Peptide analogues of Tendamistat which include the most essential residues linked by novel ω-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-Ile 61-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.

Original languageEnglish
Pages (from-to)275-280
Number of pages6
JournalProtein and Peptide Letters
Volume12
Issue number3
DOIs
StatePublished - Apr 1 2005

Keywords

  • Binding segment
  • Inhibitor
  • Linker
  • Tendamistat
  • α-amylase

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