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

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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.





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

Document Type: Research Article

DOI: https://doi.org/10.2174/092986607780782867

Publication date: 2007-05-01

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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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