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

[ Vol. 12 , Issue. 3 ]

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   Pages 275 - 280 ( 6 )

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

Affiliation:

Department of Chemistry, Eastern Michigan University, Ypsilanti, MI 48197, USA.



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