Peptide sweeteners. 6. Structural studies on the C-terminal amino acid of L-aspartyl dipeptide sweeteners
- 1 December 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Medicinal Chemistry
- Vol. 27 (12) , 1663-1668
- https://doi.org/10.1021/jm00378a023
Abstract
Stereochemical and structural aspects of the variations in the C-terminal residue of L-aspartyl-L-phenylalanine methyl ester were investigated. Novel configurational analogs such as L-aspartyl-D-alanine benzyl ester and L-aspartyl-D-.alpha.-aminobutyric acid benzyl ester were sweet. Chiral and achiral .alpha.,.alpha.-dialkylglycine and .alpha.-aminocycloakanecarboxylic acid were incorporated into the dipeptides. The L-aspartic acid based dipeptide derivatives of .alpha.-aminoisobutyric acid methyl ester, .alpha.-aminocyclopropanecarboxylic acid methyl ester, .alpha.-aminocyclobutanecarboxylic acid methyl ester and .alpha.-aminocyclopentanecarboxylic acid methyl ester were sweet. Dipeptides with .apprx.-aminocyclohexanecarboxylic acid methyl ester and .alpha.-aminocycloheptanecarboxylic acid methyl ester were bitter, whereas the analog with .alpha.-aminocylooctanecarboxylic acid methyl ester, .alpha.,.alpha.-diethylglycine methyl ester and .alpha.-aminoisobutyric acid benzyl ester were tasteless. Aspects on chirality and effective volume of the C-terminal residue are discussed and correlated with taste.This publication has 1 reference indexed in Scilit:
- Interaction of conformationally flexible agonists with the active site of sweet taste. A study of arylureasJournal of Medicinal Chemistry, 1983