Variation of pKa in the N-Terminal Tyrosine Side Chain in Octapeptide Analogs of Tendamistat Influences α-Amylase Inhibition

Author(s): D. L. Heyl, B. Sethi, A. Rogalski, C. E. Bowen, M. Lawrence, L. Beitler, E. Harning, A. Hancer, S. Sreekumar, S. Fernandes.

Journal Name: Protein & Peptide Letters

Volume 14 , Issue 5 , 2007

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Peptide analogs of tendamistat were synthesized and analyzed for α-amylase inhibitory activity. The pKa of the N-terminal tyrosine was modified by incorporation of ring-substituted analogs, which alters hydrogen bonding capacity. Ki values ranging from 70 to 524 μM generally increased with increasing pKa, indicating a necessity for H-bond donor ability.

Keywords: a-amylase, inhibitor, tendamistat, pka, hydrogen bonding, structure-activity relationship

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Article Details

Year: 2007
Page: [497 - 501]
Pages: 5
DOI: 10.2174/092986607780782867
Price: $65

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