Variation of pKa in the N-terminal tyrosine side chain in octapeptide analogs of tendamistat influences alpha-amylase inhibition.
Peptide analogs of tendamistat were synthesized and analyzed for alpha-amylase inhibitory activity. The pK(a) of the N-terminal tyrosine was modified by incorporation of ring-substituted analogs, which alters hydrogen bonding capacity. K(i) values ranging from 70 to 524 microM generally increased with increasing pK(a), indicating a necessity for H-bond donor ability.
Heyl
D L
DL
Department of Chemistry, Eastern Michigan University, Ypsilanti, MI 48197, USA. dheylcle@emich.edu
Sethi
B
B
Rogalski
A
A
Bowen
C E
CE
Lawrence
M
M
Beitler
L
L
Harning
E
E
Hancer
A
A
Sreekumar
S
S
Fernandes
S
S
D000595:Amino Acid Sequence; D007700:Kinetics; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
D010455:Peptides; D000516:alpha-Amylases; C030526:tendamistate