6331-63-1Relevant articles and documents
Candida antarctica Lipase B in a chemoenzymatic route to cyclic α-quaternary α-amino acid enantiomers
Li, Xiang-Guo,Rantapaju, Maria,Kanerva, Liisa T.
experimental part, p. 1755 - 1762 (2011/05/06)
Kinetic resolution of three cyclic quaternary ethyl 1-amino-2,3-dihydro-1H- indene-1-carboxylates and both 1- and 2-amino-1,2,3,4-tetrahydronaphthalene analogues have been studied. Interesterification with butyl butanoate and Candida antarctica lipase B accomplished the task. The enantiomers of all 1-amino analogues reacted with excellent enantioselectivity (enantiomeric ratio er greater than 200), whereas the 2-amino analogue was not enantioselective (er = 4). Amino acid enantiomers were finally obtained as their respective hydrochlorides with almost maximum theoretical yields. For the first time, a lipase enzyme was effectively used in the kinetic resolution of cyclic α-quaternary α-amino esters. Copyright
TETRALINE DERIVATIVES AS GHRELIN RECEPTOR MODULATORS
-
Page 29, (2010/02/10)
The present invention is related to compounds of formula (I), or a therapeutically suitable salt or prodrug thereof, the preparation of the compounds, compositions containing the compounds and the use of the compounds in the prevention or treatment of disorders regulated by ghrelin including anorexia, cancer cachexia, eating disorders, age-related decline in body composition, weight gain, obesity, and diabetes mellitus.
Conformationally constrained deltorphin analogs with 2-aminotetralin-2- carboxylic acid in position 3
Tóth, Géza,Darula, Zsuzsa,Péter, Antal,Fül?p, Ferenc,Tourwé, Dirk,Jaspers, Hendrika,Verheyden, Patricia,B?cskey, Zsolt,Tóth, Zoltán,Borsodi, Anna
, p. 990 - 995 (2007/10/03)
Two approaches to the design of very active and highly selective δ opioid peptides were used to obtain new deltorphin analogs with altered hydrophobic and stereoelectronic properties. Deltorphin I and II analogs were synthesized involving the substitution of Ile instead of Val at positions 5 and 6 in the address domain and 2-aminotetralin-2-carboxylic acid (Atc) instead of Phe in the message domain. The peptides were agonists in the subnanomolar range in the MVD assay and in the micromolar or higher range in the GPI assay, showing a very high selectivity for δ receptors. A very similar trend could be observed in radioreceptor binding assays in which selective tritiated opioid ligands were used. (R)- and (S)-Atc-deltorphins exhibited similar K(i) values in the binding assay, with almost complete loss of the stereospecificity of the binding. Conformational studies provided evidence for little disturbance of the backbone conformational equilibrium when Phe3 is replaced by (S)- or (R)-Atc. The use of the Atc constraint gives additional evidence that, during its interaction with the δ receptor, the side chain of residue 3 adopts the trans conformation at χ1.
