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

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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; binding segment; inhibitor; linker; tendamistat

Document Type: Review Article


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

Publication date: 2005-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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