title: Variation of pKa in the N-terminal tyrosine side chain in octapeptide analogs of tendamistat influences alpha-amylase inhibition.
abstract: 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.
authors.affiliation: Department of Chemistry, Eastern Michigan University, Ypsilanti, MI 48197, USA. dheylcle@emich.edu
authors.forename: D L
authors.initials: DL
authors.lastname: Heyl
authors.forename: B
authors.initials: B
authors.lastname: Sethi
authors.forename: A
authors.initials: A
authors.lastname: Rogalski
authors.forename: C E
authors.initials: CE
authors.lastname: Bowen
authors.forename: M
authors.initials: M
authors.lastname: Lawrence
authors.forename: L
authors.initials: L
authors.lastname: Beitler
authors.forename: E
authors.initials: E
authors.lastname: Harning
authors.forename: A
authors.initials: A
authors.lastname: Hancer
authors.forename: S
authors.initials: S
authors.lastname: Sreekumar
authors.forename: S
authors.initials: S
authors.lastname: Fernandes
mesh_terms: D000595:Amino Acid Sequence; D007700:Kinetics; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
chemical_list: D010455:Peptides; D000516:alpha-Amylases; C030526:tendamistate