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

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

Volume: 14 Issue: 5

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

Affiliation:

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

Abstract: 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.

Cite this article as:

Heyl L. D., Sethi B., Rogalski A., Bowen E. C., Lawrence M., Beitler L., Harning E., Hancer A., Sreekumar S. and Fernandes S., Variation of pKa in the N-Terminal Tyrosine Side Chain in Octapeptide Analogs of Tendamistat Influences α-Amylase Inhibition, Protein & Peptide Letters 2007; 14 (5) . https://dx.doi.org/10.2174/092986607780782867